Affinage

POT1

Protection of telomeres protein 1 · UniProt Q9NUX5

Length
634 aa
Mass
71.4 kDa
Annotated
2026-06-10
100 papers in source corpus 51 papers cited in narrative 48 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

POT1 is the single-stranded telomeric DNA-binding subunit of the shelterin complex that caps chromosome ends and prevents them from being recognized as DNA damage (PMID:11349150, PMID:15973431). Discovered first in fission yeast, where its loss causes telomere erosion and chromosome circularization (PMID:11349150), POT1 binds the G-rich 3' overhang through tandem N-terminal OB folds that clamp a minimal nonameric recognition site and protect the 3' terminus (PMID:15558049, PMID:14715659), discriminating DNA from RNA via a phenylalanine that excludes the ribose 2'-OH (PMID:20080730). It is recruited to telomeres not by direct loading alone but through its C-terminal OB/HJRL domain, which heterodimerizes with TPP1 and is thereby tethered through TIN2 to the duplex-binding shelterin proteins TRF1 and TRF2 (PMID:15231715, PMID:15181449, PMID:28393832, PMID:28393830); this TIN2-stabilized POT1-TPP1 platform is what excludes RPA from telomeric ssDNA and represses ATR kinase signaling, a pathway POT1 governs independently of TRF2's repression of ATM (PMID:17687332, PMID:18519588, PMID:22099311). POT1 caps the double-/single-stranded telomere junction by recognizing the phosphorylated 5' chromosome end through a 'POT-hole' surface, defining the precise terminal sequence (PMID:15973431, PMID:37590346). POT1 bidirectionally tunes telomerase: bound at the extreme 3' terminus it inhibits the enzyme, whereas POT1-TPP1 coating the overhang acts as a processivity factor by slowing primer dissociation and enhancing translocation, with cryo-EM revealing how TPP1-POT1 stabilizes the DNA in the telomerase active site (PMID:15792951, PMID:15632080, PMID:17237768, PMID:17237767, PMID:20094033, PMID:35201900). It resolves telomeric G-quadruplexes by conformational selection to license telomerase access (PMID:16043710, PMID:32232414), and, through phosphorylation-dependent recruitment of CST-Polα/primase, controls C-strand fill-in synthesis (PMID:27013236, PMID:38838667). POT1 also suppresses inappropriate homology-directed repair and replication-associated damage at telomeres (PMID:33073402). Germline and somatic POT1 mutations cause Coats plus disease and drive cancers by elongating telomeres or by abolishing ssDNA binding to trigger end-to-end fusions (PMID:27013236, PMID:27869160, PMID:33934394).

Mechanistic history

Synthesis pass · year-by-year structured walk · 23 steps
  1. 2001 High

    Established that a dedicated protein protects single-stranded chromosome ends, defining the founding function of POT1 before any human mechanism was known.

    Evidence Genetic deletion of pot1+ in S. pombe with in vitro ssDNA binding assays

    PMID:11349150

    Open questions at the time
    • Did not resolve how POT1 recognizes the telomeric sequence at atomic level
    • Mammalian function and complex partners unaddressed
  2. 2003 High

    Resolved the structural basis of sequence-specific ssDNA recognition, showing OB-fold loops form a clamp and specificity arises from DNA self-recognition.

    Evidence X-ray crystallography of S. pombe Pot1p N-terminal domain bound to ssDNA at 1.9 Å

    PMID:14614509

    Open questions at the time
    • Human POT1 architecture not yet defined
    • How binding relates to telomerase regulation unknown
  3. 2003 High

    Connected POT1 to telomere length homeostasis, positioning it as the terminal transducer of TRF1-mediated length signaling rather than only a passive cap.

    Evidence Co-IP, dominant-negative POT1 lacking the DNA-binding domain, and telomere length assays in human cells

    PMID:12768206 PMID:12781132

    Open questions at the time
    • Physical bridge between POT1 and TRF1 not identified
    • Direction of telomerase regulation mechanistically unresolved
  4. 2004 High

    Defined human POT1's two-OB-fold architecture, minimal recognition site, and identified TPP1/PIP1/PTOP as the adaptor that recruits POT1 to the shelterin core via TIN2.

    Evidence Crystal structure of hPOT1 N-terminus at 1.73 Å, EMSA mutagenesis, MS identification and Co-IP of TPP1/PIP1, shRNA knockdown

    PMID:14715659 PMID:15181449 PMID:15231715 PMID:15558049

    Open questions at the time
    • C-terminal domain structure and TPP1-binding interface not yet resolved
    • Mechanism of RPA exclusion not yet shown
  5. 2005 High

    Demonstrated POT1's dual biochemical roles: resolving G-quadruplexes to permit telomerase, and acting as a position-dependent bidirectional regulator of telomerase.

    Evidence Reconstituted in vitro telomerase extension and gel-shift assays with purified recombinant hPOT1

    PMID:15632080 PMID:15792951 PMID:16043710

    Open questions at the time
    • How POT1 switches from inhibitor to activator awaited the TPP1 cofactor
    • G-quadruplex resolution mechanism (induced fit vs selection) unresolved
  6. 2005 High

    Established the cellular consequence of POT1 loss—overhang erosion, loss of 5'-end sequence definition, and a G1 DNA damage response—linking POT1 to terminal structure fidelity.

    Evidence RNAi knockdown with overhang assays, DDR foci imaging, telomere sequencing, plus POT1-TRF2 Co-IP and helicase stimulation assays

    PMID:15657433 PMID:15973431 PMID:16030011

    Open questions at the time
    • Which DDR kinase POT1 represses not yet specified
    • Mechanistic basis of 5'-end definition unresolved
  7. 2006 High

    Genetic dissection in mouse revealed POT1 paralogs with separable functions—POT1a represses DDR while POT1b controls overhang length—and an aberrant HR phenotype dependent on NBS1.

    Evidence Conditional single and double knockouts in mouse cells with complementation, telomere FISH, overhang assays, NBS1 epistasis

    PMID:16839876 PMID:16839877

    Open questions at the time
    • Molecular determinants distinguishing POT1a from POT1b functions not mapped
    • Human single-gene equivalence to two mouse paralogs unclear
  8. 2007 High

    Defined POT1 as the shelterin component that specifically represses the ATR (not ATM) DNA damage pathway, and showed TPP1 binding is required for protection beyond length control.

    Evidence Conditional depletion across ATM/ATR-null backgrounds, DDR phosphorylation assays, TPP1 knockdown with POT1-variant complementation

    PMID:17632522 PMID:17687332 PMID:18535244

    Open questions at the time
    • How ATR suppression is achieved mechanistically (RPA exclusion) not yet demonstrated
    • TPP1-POT1 structural basis of telomerase switch unresolved
  9. 2007 High

    Identified TPP1 as the cofactor that converts POT1 from a telomerase inhibitor into a processivity factor, with structural similarity to ciliate TEBP-beta.

    Evidence Crystal structure of TPP1 OB domain plus reconstituted in vitro telomerase processivity assays with purified POT1-TPP1

    PMID:17237767 PMID:17237768

    Open questions at the time
    • Kinetic basis of processivity enhancement not yet dissected
    • Stoichiometry of functional POT1-TPP1 unit unknown
  10. 2009 High

    Established the mechanistic logic of telomere protection: cis ssDNA binding plus TPP1 association are jointly required to exclude RPA, and resolved how POT1 discriminates DNA from RNA.

    Evidence Separation-of-function POT1 mutants with RPA co-localization, crystallography of hPOT1 with ribouridine-substituted DNA, F62Y mutagenesis

    PMID:18519588 PMID:18955498 PMID:20008939 PMID:20080730

    Open questions at the time
    • How RPA is initially kept off versus replaced over the cell cycle unaddressed
    • TRF2 contribution to loading vs protection partially separable
  11. 2010 High

    Dissected the kinetic mechanism of telomerase stimulation, showing POT1-TPP1 acts substoichiometrically by slowing primer dissociation and enhancing translocation.

    Evidence In vitro telomerase processivity assays with purified POT1-TPP1 and kinetic step analysis

    PMID:20094033

    Open questions at the time
    • Behavior when many POT1-TPP1 coat long overhangs not yet examined
    • Structural contacts with telomerase unknown
  12. 2011 High

    Revealed cell-cycle-regulated handoff of telomeric ssDNA from RPA to POT1, orchestrated by TERRA and hnRNPA1, providing temporal control of POT1 loading.

    Evidence Purified protein assays, extract fractionation, RPA/POT1 imaging, TERRA manipulation, plus EM of POT1-TPP1-coated long ssDNA

    PMID:21399625 PMID:21596049

    Open questions at the time
    • Upstream signal triggering the switch during the cell cycle not yet defined
    • Functional role of compacted nucleoprotein structure unclear
  13. 2012 Medium

    Characterized the dynamics of POT1 and POT1-TPP1 on G-quadruplex and telomeric DNA, showing stepwise OB-fold unfolding versus TPP1-enabled sliding.

    Evidence Single-molecule FRET imaging

    PMID:22981946

    Open questions at the time
    • Single-lab smFRET not independently corroborated
    • Physiological relevance of sliding in vivo unestablished
  14. 2014 High

    Established TIN2 as the stabilizing tether that maintains TPP1/POT1 on telomeric ssDNA, and showed TIN2-tethered TPP1/POT1 is sufficient for end protection independent of TRF1.

    Evidence Conditional knockouts (TIN2, TRF1, BLM, TPP1), TIN2 allele engineering (L247E fusion), epistasis, ATR signaling assays

    PMID:22099311 PMID:24469404 PMID:25344324

    Open questions at the time
    • How phosphorylation of POT1 or partners modulates tethering unaddressed
    • Direct structural contacts within the subcomplex unresolved
  15. 2015 Medium

    Identified DNA-PKcs phosphorylation of hnRNP-A1 as the kinase signal driving the RPA-to-POT1 switch during G2/M, connecting cell-cycle kinase activity to telomere protection.

    Evidence Kinase assays, phospho-mutant expression, RPA/POT1 co-localization, DDR foci assays

    PMID:25999341

    Open questions at the time
    • Single-lab study without independent confirmation
    • Generality across cell types not established
  16. 2016 High

    Defined POT1's role in C-strand maintenance via CST and established disease mechanisms—linking the Coats plus S322L mutation and cancer OB-fold mutations to telomere fill-in failure and chromosome fusions.

    Evidence Patient and cancer mutation functional characterization, overhang/FISH assays, A-NHEJ assays, conditional KO mouse cancer models, CST/ATR epistasis

    PMID:27013236 PMID:27239034 PMID:27869160

    Open questions at the time
    • Direct structural basis of POT1-CST recruitment not yet resolved
    • How phosphorylation governs CST function unaddressed
  17. 2017 High

    Resolved the C-terminal POT1 architecture (third OB fold + HJRL domain) and the elongated POT1-TPP1 conformation, explaining how cancer mutations destabilize the complex.

    Evidence Two independent crystal structures of POT1C-TPP1 with biochemical binding and cancer-mutation characterization

    PMID:28393830 PMID:28393832

    Open questions at the time
    • Structure of POT1 bound at the ds-ss junction not yet solved
    • Telomerase-bound conformation unknown
  18. 2019 Medium

    Uncovered length-dependent telomerase inhibition by multi-POT1-TPP1 coating (via His266), TIN2's contribution to processivity, and proteostatic and tethering regulators of POT1 abundance.

    Evidence Hydroxyl-radical footprinting/MS with H266L mutant, in vitro telomerase assays with TIN2/TPP1/POT1, ubiquitination/Co-IP for TSPYL5-USP7, and SerRS pulldown/ChIP

    PMID:31278054 PMID:31383750 PMID:31685617 PMID:31815007

    Open questions at the time
    • His266 conformational switch from single-lab footprinting only
    • SerRS-POT1 tethering is Low-confidence and not independently confirmed
    • ALT-specific POT1 degradation pathway not generalized
  19. 2020 High

    Defined HDR suppression as a core human POT1 function and characterized replication-stress phenotypes, including G-quadruplex resolution by conformational selection and nuclear repositioning of dysfunctional telomeres.

    Evidence CRISPR conditional deletion in HEK293E with HDR epistasis and proteomics, biophysical G-quadruplex kinetics, BioID and nuclear F-actin imaging in POT1-mutant cells

    PMID:32232414 PMID:33073402 PMID:33122293

    Open questions at the time
    • Which HDR factors POT1 directly restrains not fully mapped
    • Trigger for nuclear-periphery relocalization mechanism incomplete
  20. 2021 High

    Distinguished the cancer-relevant consequence of POT1 mutation as telomere elongation without overt DDR, and assigned the telomerase-recruitment-enhancing role specifically to mouse POT1b.

    Evidence CRISPR engineering of caPOT1 mutations in hESCs/HSCs with in vivo competition, conditional mouse KO with POT1a/b swap and point-mutant complementation

    PMID:33934394 PMID:34535663

    Open questions at the time
    • How the three POT1b C-terminal residues mechanistically enhance recruitment not structurally defined
    • Human single-gene reconciliation of split paralog roles incomplete
  21. 2022 High

    Provided the structural mechanism of telomerase recruitment, showing how TPP1-POT1 stabilizes telomeric DNA in the active site and defines a DNA exit/anchor path governing processivity.

    Evidence Cryo-EM of human telomerase bound to TPP1 (3.2 Å) and TPP1-POT1 (3.9 Å)

    PMID:35201900

    Open questions at the time
    • Dynamics of recruitment versus the inhibitory 3'-terminal state not captured
    • How length-dependent inhibition integrates with this structure unclear
  22. 2023 High

    Solved how POT1 caps the ds-ss junction through a 'POT-hole' surface recognizing the phosphorylated 5' end, explaining 5'-end sequence definition and paralog divergence (POT1a contains it).

    Evidence Crystal structures of the POT1-junction complex with POT-hole mutagenesis and cellular ATR/end-structure assays

    PMID:37590346

    Open questions at the time
    • How junction capping coordinates with overhang coating in vivo unresolved
    • Regulation of POT-hole engagement across the cell cycle unknown
  23. 2024 High

    Defined the POT1 phospho-switch that controls CST-Polα/primase: phosphorylated POT1 holds CST inactive, and dephosphorylation releases it for C-strand fill-in synthesis.

    Evidence Cryo-EM of CST-POT1/TPP1 with phosphorylation-dependent interaction and telomere fill-in assays, disease mutation characterization

    PMID:38838667

    Open questions at the time
    • Identity of kinase/phosphatase governing the POT1 hinge switch not established
    • Temporal coordination with G-strand synthesis unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • The upstream signaling that times POT1 phosphorylation/dephosphorylation and integrates G-quadruplex resolution, junction capping, telomerase regulation, and CST fill-in into one cell-cycle program remains undefined.
  • No identified enzyme controlling the POT1 hinge phospho-switch
  • No unified model linking the cap, telomerase, and fill-in functions across the cell cycle
  • Human reconciliation of the split mouse POT1a/POT1b functions incomplete

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003677 DNA binding 6 GO:0098772 molecular function regulator activity 5 GO:0060090 molecular adaptor activity 3
Localization
GO:0000228 nuclear chromosome 3 GO:0005634 nucleus 2
Pathway
R-HSA-69306 DNA Replication 3 R-HSA-73894 DNA Repair 3 R-HSA-1640170 Cell Cycle 2
Partners
BLMCTC1-STN1-TEN1 (CST)TIN2TPP1TRF1TRF2TSPYL5WRN
Complex memberships
POT1-TPP1 heterodimershelterin

Evidence

Reading pass · 48 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 POT1 (protection of telomeres 1) protein binds the single-stranded G-rich telomeric DNA overhang at chromosome ends. Deletion of fission yeast pot1+ causes rapid loss of telomeric DNA and chromosome circularization, establishing a direct role in chromosome end protection. Genetic deletion in S. pombe (pot1+ knockout), in vitro DNA binding assays Science High 11349150
2003 Crystal structure of the N-terminal DNA-binding domain of S. pombe Pot1p complexed with single-stranded telomeric DNA at 1.9 Å resolution. The protein adopts an OB fold with two loops forming a clamp; sequence specificity arises from DNA self-recognition involving base-stacking and unusual G-T base pairs. X-ray crystallography at 1.9 Å resolution Nature High 14614509
2003 Human POT1 acts as a positive regulator of telomere length in a telomerase-dependent manner. Overexpression of hPOT1 splice variants lengthened telomeres only in telomerase-positive cells, indicating POT1 facilitates telomerase-mediated elongation. Overexpression of POT1 splice variants in telomerase-positive vs. telomerase-negative cell lines, telomere length analysis Current Biology Medium 12781132
2003 POT1 interacts with the TRF1 complex, and its binding to telomeres is regulated by TRF1 in response to telomere length. A POT1 mutant lacking the DNA-binding domain (acting as dominant negative) abrogates TRF1-mediated telomere length control and induces rapid telomere elongation, identifying POT1 as a terminal transducer of TRF1 telomere length signaling. Co-immunoprecipitation, dominant-negative POT1 expression, telomere length assays Nature High 12768206
2002 Epitope-tagged human POT1 localizes to telomeres in interphase nuclei as shown by indirect immunofluorescence. Multiple splice variants of hPOT1 exist and differ in their ability to form complexes with single-stranded telomeric DNA. Indirect immunofluorescence (EMSA for splice variant DNA binding) Molecular and Cellular Biology Medium 12391173
2004 Crystal structure of the N-terminal half of human POT1 bound to the telomeric ssDNA decamer TTAGGGTTAG at 1.73 Å resolution. hPOT1 contains two OB folds: the first binds the first six nucleotides, while the second OB fold binds and protects the 3' end of the ssDNA. X-ray crystallography at 1.73 Å resolution with in vitro binding assays Nature Structural & Molecular Biology High 15558049
2004 The minimal binding site for human POT1 on telomeric ssDNA is the nonamer 5'-TAGGGTTAG-3'. Deletion of the OB fold abolishes DNA binding. POT1 can bind internally to multimeric [TTAGGG]n arrays as well as at 3' ends. In vitro binding assays (EMSA, deletion and substitution mutants) Journal of Biological Chemistry High 14715659
2004 A novel telomeric protein PIP1 (also identified as PTOP/TPP1) binds both POT1 and TIN2, tethering POT1 to the TRF1 complex. ShRNA depletion of PIP1 or POT1 causes telomere elongation, indicating PIP1 contributes to telomere length control through POT1 recruitment. Mass spectrometry identification, co-immunoprecipitation, shRNA knockdown, telomere length assays Genes & Development High 15231715
2004 PTOP (also called PIP1/TPP1) interacts with the C-terminus of POT1 and recruits it to telomeres. RNAi-mediated inhibition of PTOP or disruption of the PTOP-POT1 interaction prevents POT1 telomeric localization and extends telomere length. Co-immunoprecipitation, RNAi knockdown, fluorescence imaging, telomere length assays Nature Cell Biology High 15181449
2005 hPOT1 disrupts telomeric G-quadruplex structures by forming a stoichiometric complex with the DNA (not catalytically), freeing the 3' tail and restoring processive telomerase elongation of G-quadruplex primers in vitro. In vitro telomerase extension assay, gel mobility shift assay with purified recombinant hPOT1 PNAS High 16043710
2005 Human POT1 acts as a negative regulator of telomerase in vitro through its DNA-binding activity. POT1 bound at the extreme 3' end of the telomere blocks telomerase, but when bound one repeat before the 3' end (leaving an 8-nt tail), it creates a preferred substrate for telomerase with improved activity and processivity. In vitro telomerase extension assay with recombinant hPOT1, crystal-structure guided positioning experiments Journal of Biological Chemistry High 15632080 15792951
2005 POT1 stimulates WRN and BLM RecQ helicases to unwind long telomeric forked duplexes and D-loop structures. This stimulation requires telomeric sequence in the duplex regions. Purified POT1 directly binds WRN and BLM in vitro. In vitro helicase assay with purified proteins, pulldown assay for protein-protein interaction Journal of Biological Chemistry High 16030011
2005 RNAi-mediated depletion of POT1 in human cells reduces the telomeric 3' overhang DNA and induces a transient DNA damage response at all telomeres in G1, but does not cause telomere fusions or cell cycle arrest. POT1 also determines the correct sequence at chromosome ends: normally the recessed 5' end ends on ATC-5', and this positional specificity is lost upon POT1 depletion. RNAi knockdown, telomere overhang assay, fluorescence imaging of DNA damage foci, telomere sequencing EMBO Journal High 15973431
2005 POT1 and TRF2 interact to form a complex with telomeric DNA. POT1 knockdown causes loss of telomeric single-stranded overhangs, apoptosis, chromosomal instability, and senescence. POT1 overexpression partially rescues TRF2-dominant-negative-induced telomere dysfunction. Co-immunoprecipitation, RNAi knockdown, overexpression rescue experiments, telomere overhang assay Molecular and Cellular Biology Medium 15657433
2006 Conditional deletion of mouse Pot1a activates a DNA damage response at telomeres, causing p53-dependent replicative senescence. Pot1a-deficient cells show overall telomere length and 3' overhang elongation and aberrant homologous recombination (telomere sister chromatid exchanges and telomere circle formation) that requires NBS1. Conditional knockout in mouse cells, genetic epistasis (NBS1 requirement), telomere FISH, telomere overhang assay Cell High 16839876
2006 Mouse telomeres contain two POT1 paralogs with distinct functions: POT1a represses a DNA damage signal at telomeres, while POT1b regulates the amount of single-stranded DNA at the telomere terminus. Double knockout causes a DNA damage signal, endoreduplication, and senescence. Conditional deletion of POT1a and/or POT1b in mouse cells, complementation experiments, telomere overhang and FISH assays Cell High 16839877
2007 Crystal structure of the TPP1 OB domain reveals structural similarity to the ciliate TEBP-beta subunit. TPP1 and POT1 form a complex that increases telomerase activity and processivity; TPP1-POT1 on telomeric DNA stimulates the telomerase core enzyme, switching from telomerase inhibition to a processivity factor role. X-ray crystallography of TPP1 OB domain, in vitro telomerase processivity assay with purified POT1-TPP1 Nature High 17237767 17237768
2007 POT1 prevents activation of ATR kinase signaling at telomeres independently of TRF2's repression of ATM. Depletion of POT1 selectively activates ATR (not ATM), while TRF2 depletion selectively activates ATM. These two shelterin proteins act independently in repressing the two DNA damage response pathways. Conditional depletion in ATM-/- and/or ATR-/- cell backgrounds (epistasis), DDR phosphorylation assays Nature High 17687332
2007 Tpp1 (TPP1 homolog in fission yeast) forms a complex with Pot1, which recruits effector molecules Ccq1 and Poz1. Poz1 bridges Pot1-Tpz1 and Taz1-Rap1, connecting single-stranded and double-stranded telomeric DNA regions, analogous to the mammalian shelterin architecture. Co-immunoprecipitation, yeast genetics, protein interaction mapping Science Medium 18535244
2007 The telomere protection function of mammalian Pot1 requires its interaction with Tpp1. Using Tpp1-knockdown cells and Pot1 variants, it was shown that Tpp1 is required for Pot1 to protect chromosome ends (suppress ATR signaling and prevent fusions), not just for telomere length regulation. RNAi knockdown of Tpp1, complementation with POT1 variants, conditional knockouts, telomere dysfunction assays Nature Structural & Molecular Biology High 17632522
2008 Domain-swap and separation-of-function analysis shows that the DNA-binding domain of POT1a specifies its ability to repress the ATR DNA damage response, while POT1b's ability to control 5'-end resection requires the TPP1-binding domain plus a region between amino acids 300–350. Human POT1 combines both functional features. Neither POT1a nor POT1b differs in in vitro DNA binding properties. Domain-swap mutagenesis, complementation of POT1a/b knockout cells, telomere damage assays Molecular and Cellular Biology High 18955498
2008 POT1 OB-fold-dependent binding to ssDNA and association with TPP1 are both required in cis for POT1 to protect telomeres and inhibit RPA localization. TRF2 binding by POT1 is dispensable for protection but promotes robust POT1 loading onto telomeric chromatin. Separation-of-function POT1 mutants, fluorescence imaging, RPA co-localization assays Molecular and Cellular Biology High 18519588
2009 TIN2 is required for the telomeric accumulation of TPP1/POT1. Upon TIN2 deletion, telomeres lose TPP1/POT1a, accumulate RPA, and activate ATR signaling. TIN2's major role is to stabilize TPP1/POT1 on ss telomeric DNA to allow RPA exclusion and ATR repression. Conditional knockout of TIN2, telomere protein localization (immunofluorescence), ATR signaling assays Molecular Cell High 22099311
2009 POT1 discriminates ssDNA over RNA via a single deoxythymidine in each telomeric repeat. A Phe62 residue creates a hydrophobic region that buries the 2'-OH of a ribouridine and eliminates favorable hydrogen bonds. TPP1 greatly augments POT1's RNA discrimination. Crystal structure of hPOT1 with a ribouridine-substituted DNA confirms the mechanism. In vitro binding assays, X-ray crystallography of hPOT1 with ribouridine-substituted DNA, site-directed mutagenesis (F62Y) PNAS High 20080730
2009 Human POT1 has higher affinity for telomeric G-rich ssDNA than RPA. Under conditions where both WRN and POT1 are limiting, both G- and C-rich telomeric strands shorten. A POT1 OB-fold fragment can restore C-strand (but not G-strand) replication in WRN-depleted cells, suggesting POT1 binding to the lagging strand template enables DNA synthesis uncoupling. RNAi knockdown of WRN and/or POT1, telomere strand-specific assays, in vitro competition binding assays Genes & Development Medium 20008939
2010 POT1-TPP1 enhances telomerase processivity by (1) slowing primer dissociation rate and (2) increasing translocation efficiency. A single POT1-TPP1-DNA interaction is necessary and sufficient. POT1-TPP1 can function substoichiometrically, supporting a recruitment function. In vitro telomerase processivity assays with purified POT1-TPP1, kinetic analysis of primer dissociation and translocation steps EMBO Journal High 20094033
2011 TERRA and hnRNPA1 orchestrate an RPA-to-POT1 switch on telomeric ssDNA. hnRNPA1 specifically displaces RPA (but not POT1) from telomeric ssDNA. TERRA inhibits this activity in early S phase; TERRA decline in late S phase unleashes hnRNPA1-mediated RPA displacement. TERRA re-accumulation after S phase promotes POT1 binding by removing hnRNPA1. Purified protein assays, cell extract fractionation, fluorescence imaging of RPA/POT1 at telomeres, TERRA manipulation experiments Nature High 21399625
2011 Multiple POT1-TPP1 heterodimers can coat long telomeric ssDNA (72–144 nt), forming compact, potentially ordered nucleoprotein structures. POT1-TPP1 (but not POT1 alone) leads to compaction of the coated ssDNA as visualized by electron microscopy. EMSA, size-exclusion chromatography, transmission electron microscopy Journal of Molecular Biology Medium 21596049
2012 POT1 unfolds G-quadruplex DNA in a stepwise, sequential manner (one OB fold at a time, 3' to 5'). In contrast, the POT1-TPP1 complex induces continuous folding and unfolding dynamics and slides back and forth on telomeric DNA, including on mutant telomeric DNA to which POT1 alone cannot bind. Single-molecule FRET (smFRET) imaging Structure Medium 22981946
2014 TRF1 deploys TIN2 and the TPP1/POT1 heterodimers to prevent ATR activation during telomere replication and repress sister telomere associations. BLM facilitates lagging-strand telomeric DNA synthesis downstream of TRF1. These are two mechanistically distinct TRF1 functions in replication. Conditional knockouts (TRF1, BLM, TPP1, Rap1) in mouse cells, epistasis analysis, TRF1/TIN2 mutant expression Genes & Development High 25344324
2014 TIN2-tethered TPP1/POT1 is sufficient for telomere protection even without TRF1 binding; when TIN2 is tethered to telomeres via TRF2 (using an artificial RCT-TIN2-L247E fusion), chromosome end protection by TRF2, TPP1/POT1a, and TPP1/POT1b is fully restored. TIN2 allele engineering (L247E mutation), fusion protein expression, conditional complementation, telomere dysfunction assays Molecular and Cellular Biology Medium 24469404
2015 DNA-PKcs phosphorylates hnRNP-A1 during G2/M phases to facilitate the RPA-to-POT1 switch on telomeric 3' overhangs. Loss of DNA-PKcs or its phosphorylation of hnRNP-A1 impairs this switch, causing DNA damage responses at telomeres during mitosis and fragile telomeres. Kinase assays, phospho-mutant expression, RPA/POT1 co-localization at telomeres, DNA damage foci assays Nucleic Acids Research Medium 25999341
2016 A POT1 S322L mutation (POT1-CP) found in Coats plus disease is defective in regulating telomerase (leading to telomere elongation) and in maintenance of the telomeric C strand, causing extended 3' overhangs and stochastic telomere truncations. POT1-CP can bind TPP1 and telomeres and block ATR signaling normally. POT1/CST-dependent telomere fill-in is implicated as the mechanism disrupted in Coats plus. Patient-derived mutation functional characterization, telomere length assays, overhang assays, telomere FISH, telomerase regulation assays, epistasis with telomerase Genes & Development High 27013236
2016 POT1 inactivation causes telomere fragility, replication fork stalling, ATR-dependent DNA damage signaling, and telomere elongation. These phenotypes are linked to impaired CST (CTC1-STN1-TEN1) function at telomeres. Cancer cells lacking POT1 function require attenuation of the ATR kinase pathway to proliferate. Conditional murine POT1a depletion in lymphoid progenitors, human/mouse cancer-associated POT1 mutation analysis, telomere replication assays, ATR pathway epistasis Cell Reports Medium 27239034
2016 Human POT1 OB-fold mutations found in cancers fail to bind ssDNA, elicit a DNA damage response, and promote chromosome fusions via alternative NHEJ (A-NHEJ). Combined conditional deletion of Pot1a/b and p53 in mouse mammary epithelium produces highly invasive breast carcinomas with telomeric breakage-fusion-bridge cycles. OB-fold mutant expression, telomere FISH, A-NHEJ assays, conditional KO mouse model Oncogene High 27869160
2017 Crystal structure of the C-terminal portion of human POT1 (POT1C) complexed with the POT1-binding motif of TPP1. POT1C contains a third OB fold and a Holliday junction resolvase-like (HJRL) domain; both domains are essential for TPP1 binding. The POT1-TPP1 complex adopts an elongated V-shaped conformation. Cancer-associated missense mutations in POT1C disrupt the POT1-TPP1 interaction, destabilize POT1, and impair telomeric DNA binding. X-ray crystallography, biochemical binding assays, cancer mutation characterization Nature Communications High 28393830 28393832
2019 POT1 His266 is a key residue mediating length-dependent regulation of telomerase. When multiple POT1-TPP1 proteins coat physiologically relevant lengths of telomeric ssDNA, they inhibit telomerase. The CLL-associated H266L mutation abrogates this inhibitory function of multi-POT1-TPP1 coating, leading to telomere overextension. Hydroxyl radical footprinting reveals conformational changes around His266 dependent on ssDNA substrate length. Hydroxyl radical footprinting coupled with mass spectrometry, in vitro telomerase assay, binding assays with H266L mutant POT1-TPP1 PNAS Medium 31685617
2019 TSPYL5 prevents poly-ubiquitination and proteasomal degradation of POT1 specifically in ALT+ cancer cells. In the absence of TSPYL5, USP7 deubiquitinase activity activates POT1 E3 ubiquitin ligase(s), promoting POT1 poly-ubiquitination. PML body environment in ALT cells potentiates POT1 degradation. Co-immunoprecipitation, ubiquitination assays, siRNA knockdown, proteasome inhibitor experiments Molecular Cell Medium 31278054
2019 SerRS (seryl tRNA synthetase) directly binds to telomeric DNA repeats in the nucleus and tethers additional POT1 proteins to telomeres through a direct interaction between the UNE-S domain of SerRS and the OB1 domain of POT1. Enrichment of POT1 at telomeres by SerRS prevents telomerase recruitment and causes progressive telomere shortening. Co-immunoprecipitation, pulldown, ChIP, telomere length assays Signal Transduction and Targeted Therapy Low 31815007
2019 TIN2 stimulates telomerase processivity in vitro, and this stimulation requires a functional TPP1 TEL patch (the telomerase-recruiting surface of TPP1), indicating TIN2 functions with TPP1/POT1 as a functional shelterin subcomplex to stimulate telomerase. In vitro telomerase processivity assay with purified TIN2/TPP1/POT1, TPP1 TEL-patch mutants Molecular and Cellular Biology Medium 31383750
2020 POT1 unfolds telomeric G-quadruplex structures via a conformational selection mechanism (not induced fit): POT1 binding is coupled to an obligatory prior unfolding of the G-quadruplex. The final complex has 2 POT1 per 24 nt DNA. Binding to folded G-quadruplex is four orders of magnitude slower than to single-stranded DNA. Stopped-flow kinetics, spectroscopic titration, isothermal calorimetry, analytical ultracentrifugation, circular dichroism, molecular dynamics simulation Nucleic Acids Research High 32232414
2020 Complete conditional deletion of POT1 in human HEK293E cells causes rapid telomere elongation and length heterogeneity, branched telomeric DNA structures, telomeric R-loops, and telomere fragility. Inactivation of homology-directed repair machinery suppresses these defects, identifying suppression of HDR as a major function of human POT1. Conditional gene deletion (CRISPR-based), telomeric chromatin isolation proteomics, epistasis with HDR pathway inhibitors, telomere FISH EMBO Journal High 33073402
2020 POT1 dysfunction (mutations) causes replication stress manifesting as increased mitotic DNA synthesis at telomeres. Depletion of nuclear pore complex (NPC) subunits worsens telomere damage in POT1-mutant cells. Mutant-POT1-expressing cells relocalize dysfunctional telomeres to the nuclear periphery via nuclear F-actin polymerization. CRISPR interference, biotin-based proximity labeling (BioID), nuclear pore subunit depletion, nuclear F-actin imaging Genes & Development Medium 33122293
2021 Cancer-associated POT1 mutations engineered into human embryonic stem cells and hematopoietic stem cells cause telomere elongation without detectable telomere damage response or ATR signaling. This indicates caPOT1 mutations are selected in cancer for their ability to elongate telomeres rather than for induction of DNA damage. CRISPR engineering of cancer-associated POT1 mutations in hESCs and HSCs, telomere damage assays, competition experiments in vitro and in vivo EMBO Journal High 33934394
2021 Mouse POT1b (but not POT1a) enhances telomerase recruitment to telomeres through three specific amino acids in its TPP1-interacting C-terminus, coordinating G-strand synthesis. POT1a conversely negatively regulates telomere length by inhibiting telomerase recruitment. Conditional mouse KO, complementation with POT1a/b swap mutants and point mutants, telomere length assays, telomerase recruitment assays Nature Communications High 34535663
2022 Cryo-EM structures of human telomerase bound to TPP1 (3.2 Å) and to TPP1-POT1 (3.9 Å) reveal the interactions required for telomerase recruitment. TPP1-POT1 stabilizes the telomeric DNA in the active site, reveals an unexpected DNA exit path and a DNA anchor site on telomerase important for processivity. Cryo-electron microscopy at 3.2–3.9 Å resolution Science High 35201900
2023 Human POT1 caps the telomeric double-stranded/single-stranded (ds-ss) DNA junction by recognizing the phosphorylated 5' end of the chromosome via a 'POT-hole' surface. Crystal structures reveal the structural basis of junction binding. Mutation of the POT-hole compromises junction protection in vitro and leads to loss of telomeric 5'-end definition and ATR-DDR induction in cells. Mouse POT1a (not POT1b) contains the POT-hole and binds the junction, explaining why POT1a is sufficient for end protection. X-ray crystallography of POT1-junction complex, in vitro binding assays, POT-hole mutagenesis, human cell ATR signaling and telomere end-structure assays Science High 37590346
2024 Cryo-EM structures of human CST bound to the shelterin heterodimer POT1/TPP1 reveal how CST is recruited to telomeres by POT1. POT1 hinge phosphorylation is required for CST recruitment. Phosphorylated POT1 holds CST-Polα/primase in an inactive (autoinhibited) state; dephosphorylation of POT1 releases CST-Polα/primase into an active state to perform C-strand fill-in synthesis. Cryo-electron microscopy structure of CST-POT1/TPP1, biochemical assays for POT1 phosphorylation-dependent CST interactions, functional telomere fill-in assays Cell High 38838667

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Pot1, the putative telomere end-binding protein in fission yeast and humans. Science (New York, N.Y.) 815 11349150
2007 Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1. Nature 705 17687332
2007 The POT1-TPP1 telomere complex is a telomerase processivity factor. Nature 561 17237768
2003 POT1 as a terminal transducer of TRF1 telomere length control. Nature 550 12768206
2007 TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. Nature 390 17237767
2004 Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection. Nature structural & molecular biology 384 15558049
2004 POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex. Genes & development 354 15231715
2004 PTOP interacts with POT1 and regulates its localization to telomeres. Nature cell biology 350 15181449
2006 Pot1 deficiency initiates DNA damage checkpoint activation and aberrant homologous recombination at telomeres. Cell 332 16839876
2006 Recent expansion of the telomeric complex in rodents: Two distinct POT1 proteins protect mouse telomeres. Cell 320 16839877
2014 POT1 loss-of-function variants predispose to familial melanoma. Nature genetics 319 24686849
2005 Human POT1 disrupts telomeric G-quadruplexes allowing telomerase extension in vitro. Proceedings of the National Academy of Sciences of the United States of America 315 16043710
2009 RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway. Molecular cell 286 19854130
2011 TERRA and hnRNPA1 orchestrate an RPA-to-POT1 switch on telomeric single-stranded DNA. Nature 282 21399625
2014 Rare missense variants in POT1 predispose to familial cutaneous malignant melanoma. Nature genetics 278 24686846
2005 POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end. The EMBO journal 241 15973431
2013 POT1 mutations cause telomere dysfunction in chronic lymphocytic leukemia. Nature genetics 232 23502782
2011 Telomere protection by TPP1/POT1 requires tethering to TIN2. Molecular cell 189 22099311
2008 Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere length. Science (New York, N.Y.) 186 18535244
2006 The G-quadruplex ligand telomestatin inhibits POT1 binding to telomeric sequences in vitro and induces GFP-POT1 dissociation from telomeres in human cells. Cancer research 170 16849533
2003 Human POT1 facilitates telomere elongation by telomerase. Current biology : CB 170 12781132
2003 DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA. Nature 168 14614509
2005 Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro. Molecular and cellular biology 161 15632080
2005 POT1 stimulates RecQ helicases WRN and BLM to unwind telomeric DNA substrates. The Journal of biological chemistry 157 16030011
2014 TRF1 negotiates TTAGGG repeat-associated replication problems by recruiting the BLM helicase and the TPP1/POT1 repressor of ATR signaling. Genes & development 156 25344324
2007 Telomere protection by mammalian Pot1 requires interaction with Tpp1. Nature structural & molecular biology 152 17632522
2010 POT1-TPP1 enhances telomerase processivity by slowing primer dissociation and aiding translocation. The EMBO journal 144 20094033
2002 Human Pot1 (protection of telomeres) protein: cytolocalization, gene structure, and alternative splicing. Molecular and cellular biology 141 12391173
2015 A mutation in the POT1 gene is responsible for cardiac angiosarcoma in TP53-negative Li-Fraumeni-like families. Nature communications 139 26403419
2005 Switching human telomerase on and off with hPOT1 protein in vitro. The Journal of biological chemistry 135 15792951
2005 POT1 and TRF2 cooperate to maintain telomeric integrity. Molecular and cellular biology 131 15657433
2004 DNA binding features of human POT1: a nonamer 5'-TAGGGTTAG-3' minimal binding site, sequence specificity, and internal binding to multimeric sites. The Journal of biological chemistry 131 14715659
2004 Loss of hPot1 function leads to telomere instability and a cut-like phenotype. Current biology : CB 119 15620654
2012 POT1-TPP1 regulates telomeric overhang structural dynamics. Structure (London, England : 1993) 108 22981946
2016 Complex karyotypes and KRAS and POT1 mutations impact outcome in CLL after chlorambucil-based chemotherapy or chemoimmunotherapy. Blood 104 27226433
2008 Functional dissection of human and mouse POT1 proteins. Molecular and cellular biology 101 18955498
2016 Telomere Replication Stress Induced by POT1 Inactivation Accelerates Tumorigenesis. Cell reports 98 27239034
2004 Expression of POT1 is associated with tumor stage and telomere length in gastric carcinoma. Cancer research 93 14744765
2017 Structural and functional analysis of the human POT1-TPP1 telomeric complex. Nature communications 86 28393830
2016 A POT1 mutation implicates defective telomere end fill-in and telomere truncations in Coats plus. Genes & development 86 27013236
2017 Structural insights into POT1-TPP1 interaction and POT1 C-terminal mutations in human cancer. Nature communications 82 28393832
2022 Structural basis of human telomerase recruitment by TPP1-POT1. Science (New York, N.Y.) 80 35201900
2010 Single molecule studies of physiologically relevant telomeric tails reveal POT1 mechanism for promoting G-quadruplex unfolding. The Journal of biological chemistry 75 21183684
2002 Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe. Biochemistry 75 12463756
2017 The wide spectrum of POT1 gene variants correlates with multiple cancer types. European journal of human genetics : EJHG 69 28853721
2014 TRF2-tethered TIN2 can mediate telomere protection by TPP1/POT1. Molecular and cellular biology 68 24469404
2004 Rescue of an hTERT mutant defective in telomere elongation by fusion with hPot1. Molecular and cellular biology 64 15060173
2006 Vertebrate POT1 restricts G-overhang length and prevents activation of a telomeric DNA damage checkpoint but is dispensable for overhang protection. Molecular and cellular biology 59 16943437
2010 Pot1 and telomere maintenance. FEBS letters 57 20493859
2015 DNA-PKcs phosphorylates hnRNP-A1 to facilitate the RPA-to-POT1 switch and telomere capping after replication. Nucleic acids research 54 25999341
2007 Pot1 and cell cycle progression cooperate in telomere length regulation. Nature structural & molecular biology 54 18066078
2020 Replication stress conferred by POT1 dysfunction promotes telomere relocalization to the nuclear pore. Genes & development 52 33122293
2009 How telomeric protein POT1 avoids RNA to achieve specificity for single-stranded DNA. Proceedings of the National Academy of Sciences of the United States of America 52 20080730
2020 Role of POT1 in Human Cancer. Cancers 51 32987645
2016 Pot1 OB-fold mutations unleash telomere instability to initiate tumorigenesis. Oncogene 51 27869160
2010 The protein network surrounding the human telomere repeat binding factors TRF1, TRF2, and POT1. PloS one 51 20811636
2013 Cancer chromosomes going to POT1. Nature genetics 49 23619786
2009 Human POT1 is required for efficient telomere C-rich strand replication in the absence of WRN. Genes & development 49 20008939
2021 Cancer-associated POT1 mutations lead to telomere elongation without induction of a DNA damage response. The EMBO journal 47 33934394
2019 TSPYL5 Depletion Induces Specific Death of ALT Cells through USP7-Dependent Proteasomal Degradation of POT1. Molecular cell 47 31278054
2009 Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1. The Journal of biological chemistry 46 19734539
2020 POT1 mutation spectrum in tumour types commonly diagnosed among POT1-associated hereditary cancer syndrome families. Journal of medical genetics 44 31937561
2020 Human shelterin protein POT1 prevents severe telomere instability induced by homology-directed DNA repair. The EMBO journal 43 33073402
2020 POT1-TPP1 telomere length regulation and disease. Computational and structural biotechnology journal 42 32774788
2019 POT1 germline mutations but not TERT promoter mutations are implicated in melanoma susceptibility in a large cohort of Spanish melanoma families. The British journal of dermatology 42 30451293
2019 TIN2 Functions with TPP1/POT1 To Stimulate Telomerase Processivity. Molecular and cellular biology 42 31383750
2005 Distinct requirements for Pot1 in limiting telomere length and maintaining chromosome stability. Molecular and cellular biology 42 15964812
2020 A Germline Mutation in the POT1 Gene Is a Candidate for Familial Non-Medullary Thyroid Cancer. Cancers 39 32492864
2013 The shelterin protein POT-1 anchors Caenorhabditis elegans telomeres through SUN-1 at the nuclear periphery. The Journal of cell biology 37 24297748
2019 Association of the POT1 Germline Missense Variant p.I78T With Familial Melanoma. JAMA dermatology 36 30586141
2017 A new POT1 germline mutation-expanding the spectrum of POT1-associated cancers. Familial cancer 36 28389767
2023 Human POT1 protects the telomeric ds-ss DNA junction by capping the 5' end of the chromosome. Science (New York, N.Y.) 35 37590346
2021 Distinct functions of POT1 proteins contribute to the regulation of telomerase recruitment to telomeres. Nature communications 35 34535663
2020 Insights into Genetic Susceptibility to Melanoma by Gene Panel Testing: Potential Pathogenic Variants in ACD, ATM, BAP1, and POT1. Cancers 34 32325837
2011 Multiple POT1-TPP1 proteins coat and compact long telomeric single-stranded DNA. Journal of molecular biology 34 21596049
2008 Distinct functions of POT1 at telomeres. Molecular and cellular biology 32 18519588
2022 Telomere dysfunction implicates POT1 in patients with idiopathic pulmonary fibrosis. The Journal of experimental medicine 31 35420632
2010 Pot1 inactivation leads to rampant telomere resection and loss in one cell cycle. Nucleic acids research 31 20601686
2020 Human POT1 unfolds G-quadruplexes by conformational selection. Nucleic acids research 30 32232414
2009 POT1 proteins in green algae and land plants: DNA-binding properties and evidence of co-evolution with telomeric DNA. Nucleic acids research 30 19783822
2008 Mechanism and substrate specificity of telomeric protein POT1 stimulation of the Werner syndrome helicase. Nucleic acids research 30 18583366
2008 Splenic marginal zone lymphomas are characterized by loss of interstitial regions of chromosome 7q, 7q31.32 and 7q36.2 that include the protection of telomere 1 (POT1) and sonic hedgehog (SHH) genes. British journal of haematology 29 18492102
2009 POT1 association with TRF2 regulates telomere length. Molecular and cellular biology 26 19651898
2019 POT1-TPP1 differentially regulates telomerase via POT1 His266 and as a function of single-stranded telomere DNA length. Proceedings of the National Academy of Sciences of the United States of America 25 31685617
2012 RPA and POT1: friends or foes at telomeres? Cell cycle (Georgetown, Tex.) 25 22373525
2009 POT1-independent single-strand telomeric DNA binding activities in Brassicaceae. The Plant journal : for cell and molecular biology 25 19228335
1992 The POT1 gene for yeast peroxisomal thiolase is subject to three different mechanisms of regulation. Molecular microbiology 25 1354832
2024 POT1 recruits and regulates CST-Polα/primase at human telomeres. Cell 24 38838667
2020 Genetic variation in POT1 and risk of thyroid subsequent malignant neoplasm: A report from the Childhood Cancer Survivor Study. PloS one 24 32040538
2020 MiR-185 targets POT1 to induce telomere dysfunction and cellular senescence. Aging 24 32687062
2019 Seryl tRNA synthetase cooperates with POT1 to regulate telomere length and cellular senescence. Signal transduction and targeted therapy 24 31815007
2017 The telomere binding protein Pot1 maintains haematopoietic stem cell activity with age. Nature communications 24 28986560
2013 Caenorhabditis elegans POT-1 and POT-2 repress telomere maintenance pathways. G3 (Bethesda, Md.) 23 23390606
2011 DNA-induced dimerization of the single-stranded DNA binding telomeric protein Pot1 from Schizosaccharomyces pombe. Nucleic acids research 23 21911358
2016 POT1-TPP1 Binding and Unfolding of Telomere DNA Discriminates against Structural Polymorphism. Journal of molecular biology 22 27173378
2017 POT1-mediated δ-integration strategy for high-copy, stable expression of heterologous proteins in Saccharomyces cerevisiae. FEMS yeast research 21 28922845
2010 Altered mRNA expression of telomere binding proteins (TPP1, POT1, RAP1, TRF1 and TRF2) in ulcerative colitis and Crohn's disease. Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 21 20061197
2012 Interaction of Berberine derivative with protein POT1 affect telomere function in cancer cells. Biochemical and biophysical research communications 19 22369941
2023 POT1 mutations cause differential effects on telomere length leading to opposing disease phenotypes. Journal of cellular physiology 18 37183325
2018 Germline Variants in the POT1-Gene in High-Risk Melanoma Patients in Austria. G3 (Bethesda, Md.) 18 29523635

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