Affinage

AP2M1

AP-2 complex subunit mu · UniProt Q96CW1

Round 2 corrected
Length
435 aa
Mass
49.7 kDa
Annotated
2026-04-28
130 papers in source corpus 35 papers cited in narrative 34 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

AP2M1 (μ2) is the cargo-recognition subunit of the heterotetrameric AP-2 clathrin adaptor complex and functions as a central hub for clathrin-mediated endocytosis by directly binding YXXφ and FDNPVY tyrosine-based sorting signals on transmembrane cargo proteins through two distinct sites on its C-terminal domain, while its N-terminal domain anchors it within the AP-2 core (PMID:7569928, PMID:9812899, PMID:12121421). Phosphorylation of Thr156 by AAK1 and LRRK2 triggers a conformational change that exposes the otherwise buried cargo-binding site, and a conserved lysine cluster mediates PI(4,5)P₂-dependent membrane recruitment, together gating productive coated-vesicle formation (PMID:8257432, PMID:12086608, PMID:12119359, PMID:34315807). AP2M1 is required for endocytosis of transferrin receptor, CTLA-4, claudin-2, N-cadherin, Na⁺/K⁺-ATPase, SLC26A4, and ferritin, and is broadly exploited by viruses (HCV, influenza A, Zika, SARS-CoV-2, HPV-16 E7) that hijack its YXXφ-binding pocket for intracellular trafficking of viral proteins (PMID:10228163, PMID:9200449, PMID:34964704, PMID:28224728, PMID:22916011, PMID:32923629, PMID:36255238). A recurrent de novo p.Arg170Trp missense variant causes developmental and epileptic encephalopathy by impairing AP-2 conformational activation and clathrin-mediated endocytosis (PMID:31104773).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 1988 Medium

    Molecular cloning of AP50 (AP2M1) from rat brain established its identity as a 435-amino-acid structural component of the AP-2 clathrin adaptor complex, providing the first primary sequence for a medium adaptor chain.

    Evidence cDNA cloning and sequencing from rat brain cDNA library

    PMID:3148444

    Open questions at the time
    • no functional role assigned beyond structural component
    • no binding partners or cargo specificity identified
  2. 1993 High

    Identification of Thr156 as the sole phosphorylation site on AP2M1 by a co-purifying kinase established that μ2 is a regulated subunit, though the functional significance of this modification remained unknown.

    Evidence In vitro phosphorylation with tryptic peptide mapping and Edman degradation

    PMID:8257432

    Open questions at the time
    • identity of the endogenous kinase unresolved
    • in vivo phosphorylation significance unknown
    • no link to cargo binding or endocytosis established
  3. 1995 High

    The discovery that μ1 and μ2 medium chains directly bind YXXφ tyrosine-based sorting signals resolved a long-standing question of which AP subunit recognizes cargo, establishing AP2M1 as the signal-recognition component of the clathrin machinery.

    Evidence Yeast two-hybrid screen confirmed by in vitro binding assays

    PMID:7569928

    Open questions at the time
    • structural basis of recognition unknown
    • whether μ2 recognizes non-YXXφ signals unclear
  4. 1997 High

    Domain mapping revealed AP2M1's bipartite architecture — an N-terminal domain for AP-2 core assembly and a C-terminal domain for cargo binding — while quantitative biophysics measured ~58 nM affinity for YXXφ peptides, and CTLA-4 was identified as an immunologically important cargo.

    Evidence Yeast two-hybrid domain mapping, optical biosensor Kd determination, CTLA-4 mutagenesis and co-immunoprecipitation

    PMID:9162036 PMID:9200449 PMID:9341158

    Open questions at the time
    • no three-dimensional structure available
    • phosphorylation-dependent regulation of cargo binding untested
  5. 1998 High

    Crystal structures of the μ2 C-terminal domain complexed with YXXφ peptides at 2.7 Å revealed the atomic basis of signal recognition — cargo peptides adopt an extended conformation engaging hydrophobic pockets — answering how selectivity for tyrosine and bulky hydrophobic residues is achieved.

    Evidence X-ray crystallography at 2.7 Å with EGFR and TGN38 peptides

    PMID:9812899

    Open questions at the time
    • no structure of full AP-2 complex available
    • how cargo-binding site becomes accessible in vivo unknown
  6. 1999 High

    Dominant-negative μ2 mutations (D176A/W421A) demonstrated that cargo-binding-site integrity is essential for transferrin receptor endocytosis but dispensable for EGF receptor internalization, establishing cargo selectivity of the AP2M1-dependent pathway.

    Evidence Inducible expression of mutant μ2 with metabolic replacement and endocytosis assays

    PMID:10228163

    Open questions at the time
    • alternative adaptors for EGF receptor unidentified
    • in vivo significance in organismal physiology not tested
  7. 2002 High

    Three key advances converged: the full AP-2 core crystal structure showed the YXXφ site on μ2 is buried in the inactive conformation, requiring a conformational switch; a PI(4,5)P₂-binding lysine cluster on μ2 was shown to be required for membrane recruitment; and a second distinct binding site for the FDNPVY motif of LDLR was identified, establishing μ2 as a multi-site, allosterically regulated cargo adaptor.

    Evidence X-ray crystallography of AP-2 core at 2.6 Å; liposome binding and dominant-negative PI(4,5)P₂ mutants; surface plasmon resonance and photoactivated crosslinking

    PMID:12086608 PMID:12119359 PMID:12121421

    Open questions at the time
    • direct demonstration that Thr156 phosphorylation triggers the conformational switch in cells still lacking
    • structural basis of FDNPVY recognition unresolved
  8. 2003 High

    siRNA knockdown of μ2 reduced clathrin-coated pits ~12-fold and blocked transferrin uptake but not LDL or EGF receptor internalization, confirming AP2M1 is essential for coated-pit formation and demonstrating cargo-specific redundancy among endocytic adaptors.

    Evidence RNAi to undetectable levels with EM and multiple cargo endocytosis assays

    PMID:12952941

    Open questions at the time
    • identity of compensatory adaptors for LDL/EGF receptor unclear
    • organismal knockout phenotype not yet available
  9. 2004 High

    Linking AP2M1 phosphorylation to a physiological output, hyperphosphorylation of μ2 driven by hypertensive α-adducin variants was shown to impair AP-2 binding to Na⁺/K⁺-ATPase and block dopamine-stimulated ATPase endocytosis in renal cells, establishing μ2 phosphorylation as a regulated step in ion-transporter trafficking.

    Evidence Expression of adducin variants in renal epithelial cells with co-IP and ATPase activity assays

    PMID:15528469

    Open questions at the time
    • whether this mechanism contributes to human hypertension in vivo not confirmed
    • kinase identity for pathological hyperphosphorylation not fully resolved
  10. 2006 High

    AAK1 was confirmed as a physiological Thr156 kinase whose activity is essential for Na⁺/K⁺-ATPase endocytosis in response to dopamine and hypoxia-ROS, while systematic mutagenesis showed that no single μ2 binding-site mutation abolishes AP-2 function, indicating functional redundancy among interaction surfaces.

    Evidence Phosphorylation-site mutagenesis (T156A), kinase inhibitors, siRNA replacement genetics with transferrin uptake

    PMID:16498080 PMID:17035630

    Open questions at the time
    • whether additional kinases phosphorylate Thr156 in neurons not addressed
    • structural basis of conformational activation upon phosphorylation unresolved
  11. 2008 High

    The cargo repertoire of AP2M1 was extended to include ferritin uptake in intestinal cells and the α1b-adrenergic receptor, while C. elegans genetics showed that the μ2 ortholog facilitates but is not absolutely required for synaptic vesicle recycling.

    Evidence RNAi with ferritin uptake in Caco-2; Co-IP with α1b-AR; C. elegans apm-2 loss-of-function with EM and electrophysiology

    PMID:18356317 PMID:18523139 PMID:19047463

    Open questions at the time
    • whether mammalian synaptic vesicle recycling shows similar partial dependence untested
    • structural basis of ferritin recognition not characterized
  12. 2012 High

    HCV core protein was shown to hijack AP2M1 via a YXXφ motif to achieve viral assembly on lipid droplets; AAK1 and GAK kinases regulate this interaction, revealing AP2M1 as a druggable host factor for viral infection.

    Evidence Microfluidics affinity analysis, protein-fragment complementation, siRNA, dominant-negative μ2, infectivity assays

    PMID:22916011

    Open questions at the time
    • whether kinase inhibitors have therapeutic efficacy in patients not tested
    • structural details of core–μ2 interaction unresolved
  13. 2017 High

    AP2M1 was shown to mediate clathrin-dependent endocytosis of N-cadherin via two YXXφ motifs masked by β-catenin, linking AP2M1 to cell-adhesion dynamics and neurite outgrowth.

    Evidence Co-IP, YXXφ mutagenesis, live-cell endocytosis, neurite outgrowth quantification

    PMID:28224728

    Open questions at the time
    • in vivo neuronal phenotype of this specific interaction untested
    • whether other cadherins share this regulatory mechanism unknown
  14. 2019 High

    A recurrent de novo p.Arg170Trp variant in AP2M1 was identified as causative for developmental and epileptic encephalopathy, establishing the first Mendelian disease linked to μ2; the mutation impairs conformational activation without affecting protein stability or membrane recruitment.

    Evidence Whole-exome sequencing, molecular dynamics, functional complementation in human cells and mouse astrocytes

    PMID:31104773

    Open questions at the time
    • complete patient cohort phenotypic spectrum not fully delineated
    • whether residual AP-2 function in patients is cargo-selective not tested
  15. 2020 High

    AP2M1 was established as a broadly exploited host factor across diverse virus families (influenza A, Zika, HIV, MERS-CoV, SARS-CoV-2, EV-A71) via YXXφ-mediated interactions, and the small molecule ACA was shown to disrupt these interactions and inhibit viral replication in vivo.

    Evidence YXXφ mutagenesis, AP2M1 siRNA, immunofluorescence, in vitro and in vivo antiviral assays

    PMID:32923629

    Open questions at the time
    • ACA selectivity and off-target effects not fully characterized
    • whether all viral YXXφ motifs bind the same μ2 pocket not structurally resolved
  16. 2021 High

    LRRK2 was identified as a second direct Thr156 kinase; bidirectional dysregulation of AP2M1 phosphorylation by LRRK2 loss- or gain-of-function impairs CCV dynamics and contributes to dopaminergic neurodegeneration in a Drosophila PD model, linking AP2M1 to Parkinson's disease pathogenesis.

    Evidence Co-IP, kinase assay, mouse brain tissue analysis, Drosophila neurodegeneration model

    PMID:34315807

    Open questions at the time
    • whether LRRK2-mediated μ2 phosphorylation is altered in human PD brain tissue not shown
    • relative contributions of AAK1 vs LRRK2 in neurons not quantified
  17. 2021 High

    AP2M1 was found to bridge clathrin-mediated endocytosis and autophagy by binding claudin-2 via YXXφ motifs and interacting with LC3, coupling starvation-induced CLDN2 internalization to autophagosomal degradation and tight junction remodeling.

    Evidence Co-IP, CRISPR knockout, YXXφ mutagenesis, in vivo mouse and ex vivo human colon validation

    PMID:34964704

    Open questions at the time
    • structural basis of μ2–LC3 interaction unknown
    • whether other tight junction proteins are similarly regulated via AP2M1–autophagy coupling not tested
  18. 2022 High

    HPV-16 E7 was shown to bind AP2M1 via a YXXφ-like motif to inhibit AP-2-mediated EGFR internalization, contributing to cellular transformation independently of pRB binding.

    Evidence Mutagenesis of Y25, co-IP, CKII phosphorylation, EGFR internalization and transformation assays

    PMID:36255238

    Open questions at the time
    • whether other HPV types use the same mechanism not tested
    • contribution of E7–AP2M1 to in vivo tumorigenesis not established
  19. 2024 High

    AP2M1 was shown to regulate SLC26A4 (Pendrin) plasma membrane abundance in the endolymphatic sac via CME, extending the endocytic cargo repertoire to inner ear ion transport.

    Evidence Co-localization, structural modeling with experimental validation, pharmacological CME inhibition in native tissue

    PMID:39383236

    Open questions at the time
    • whether AP2M1-mediated SLC26A4 endocytosis contributes to Pendred syndrome pathology not tested
    • direct binding site on SLC26A4 not mapped by mutagenesis

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: the structural basis of the full conformational transition upon Thr156 phosphorylation at atomic resolution; the relative contributions of AAK1 vs LRRK2 to μ2 phosphorylation in different tissues; the structural determinants of the FDNPVY-binding site; and whether AP2M1–LC3 coupling represents a general mechanism linking CME to selective autophagy.
  • no high-resolution structure of open/active full AP-2 with phospho-Thr156
  • tissue-specific kinase hierarchy for Thr156 not quantified
  • FDNPVY-binding site structural details unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0038024 cargo receptor activity 6 GO:0060090 molecular adaptor activity 3 GO:0008289 lipid binding 2
Localization
GO:0005886 plasma membrane 5 GO:0031410 cytoplasmic vesicle 4 GO:0005811 lipid droplet 1
Pathway
R-HSA-5653656 Vesicle-mediated transport 11 R-HSA-1643685 Disease 4 R-HSA-168256 Immune System 3 R-HSA-382551 Transport of small molecules 3 R-HSA-112316 Neuronal System 2 R-HSA-9612973 Autophagy 1
Partners
AAK1AP2B1CDH2CLDN2CTLA4LRRK2SLC26A4SYT1
Complex memberships
AP-2 adaptor complex

Evidence

Reading pass · 34 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 The medium chains μ1 and μ2 of clathrin-associated adaptor complexes AP-1 and AP-2 specifically interact with tyrosine-based sorting signals (YXXφ motifs) in the cytoplasmic domains of integral membrane proteins, identifying them as the signal-binding components of the clathrin-dependent sorting machinery. Yeast two-hybrid screen confirmed by in vitro binding assays Science High 7569928
1997 The AP2M1 (AP50/μ2) subunit of AP-2 directly binds the cytoplasmic YVKM motif of CTLA-4 via tyrosine-dependent interaction, mediating ligand-independent endocytosis of CTLA-4 into clathrin-coated vesicles and limiting its cell surface expression. Yeast two-hybrid, co-immunoprecipitation, site-directed mutagenesis (Y201F), cell surface expression assays Journal of Immunology High 9200449 9256472
1997 AP2M1 has a bipartite domain structure: the N-terminal one-third (residues ~1–145) mediates assembly with the β2 chain of the AP-2 complex, while the C-terminal two-thirds (residues ~164–435) binds tyrosine-based sorting signals. Yeast two-hybrid domain mapping and proteolytic digestion experiments The Journal of Biological Chemistry High 9341158
1997 AP2M1 interacts with TGN38's internalization motif (SDYQRL) through an absolute requirement for Tyr-333; additionally Ser-331 contributes to binding affinity. The dissociation constant for the μ2–TGN38 cytosolic tail interaction was determined to be ~58 nM. Yeast two-hybrid, in vitro fusion protein binding, IAsys optical biosensor, tryptophan fluorescence equilibrium measurement The Journal of Biological Chemistry High 9162036
1998 Crystal structures of the internalization-signal binding domain of μ2 (AP2M1) complexed with YXXΦ peptides from EGFR and TGN38 at 2.7 Å resolution revealed that signal peptides adopt an extended conformation, with specificity conferred by hydrophobic pockets binding the tyrosine and leucine residues. X-ray crystallography at 2.7 Å resolution Science High 9812899
1999 Asp176 and Trp421 of AP2M1 are critical residues for interaction with tyrosine-based internalization motifs; mutation of both to alanine (dominant-negative μ2) causes metabolic replacement of endogenous μ2 in AP-2, abrogates AP-2/tyrosine-motif interactions, and severely impairs transferrin receptor endocytosis while leaving EGF receptor internalization unaffected. Inducible overexpression of epitope-tagged dominant-negative μ2 mutants, endocytosis assays, metabolic replacement assay The EMBO Journal High 10228163
2000 The C2B domain of synaptotagmin binds both μ2 (AP2M1) and α-adaptin subunits of the AP-2 complex; μ2 is the major interacting subunit and binds synaptotagmin at a site in subdomain B distinct from the tyrosine-motif binding site. Synaptotagmin at the liposome surface enhances AP-2 and clathrin recruitment, and perturbation of synaptotagmin–AP-2 interaction inhibits transferrin internalization, demonstrating a role in nucleating endocytic clathrin-coated pits. Co-immunoprecipitation, liposome recruitment assay, dominant-negative perturbation, transferrin internalization assay The EMBO Journal High 11080148
2002 AP2M1 contains a conserved phosphatidylinositol-(4,5)-bisphosphate (PI(4,5)P2) binding site constituted by a cluster of conserved lysine residues; mutations abolishing PI(4,5)P2 binding prevent AP-2/clathrin recruitment to PI(4,5)P2-containing liposomes or presynaptic membranes and inhibit receptor-mediated endocytosis in living cells. Lipid-binding assays with liposomes, competition assays with presynaptic membranes, dominant-negative expression with endocytosis assays The Journal of Cell Biology High 12119359
2002 AP2M1 binds the FDNPVY internalization signal of the LDL receptor at a site distinct from the site that recognizes the general YXXφ (YppΦ) sorting signal, demonstrating that μ2 has at least two separate cargo-binding sites. Surface plasmon resonance and photoactivated crosslinking with peptide probes Traffic High 12121421
2002 The crystal structure of the full AP-2 core complex (α-trunk, β2-trunk, μ2, σ2) at 2.6 Å shows two potential polyphosphoinositide binding sites (on α and μ2); the YXXφ motif binding site on AP2M1 is buried in the inactive conformation, indicating that a conformational change—likely triggered by phosphorylation in the disordered μ2 linker—is required to expose the cargo-binding site. X-ray crystallography at 2.6 Å resolution of AP-2 core complex Cell High 12086608
2003 AP2M1 (μ2) knockdown by siRNA reduces clathrin-coated pit abundance ~12-fold and severely inhibits transferrin receptor-mediated endocytosis; however EGF receptor and LDL receptor internalization are unaffected in AP-2-depleted cells, indicating AP-2/μ2 is required for specific cargo but that alternative adaptors can substitute for others. RNA interference knockdown to undetectable levels, electron microscopy, transferrin/EGF/LDL receptor endocytosis assays The Journal of Cell Biology High 12952941
2004 Hypertension-associated α-adducin mutation causes hyperphosphorylation of the AP2M1 (μ2) subunit, which prevents AP-2 from binding the Na+,K+-ATPase α-subunit and thereby impairs dopamine-stimulated Na+,K+-ATPase endocytosis in renal tubule cells, identifying AP2M1 phosphorylation as a regulated step in Na+,K+-ATPase trafficking. Expression of hypertensive adducin variants in renal epithelial cells, co-immunoprecipitation, ATPase activity measurements, endocytosis assays Circulation Research High 15528469
2006 Phosphorylation of AP2M1 (μ2) at Thr156 by adaptor-associated kinase 1 (AAK1)/PKC-ζ is essential for Na+,K+-ATPase endocytosis in response to dopamine and hypoxia-generated ROS; a T156A phosphorylation-site mutant of μ2 prevents Na+,K+-ATPase endocytosis and the associated changes in ATPase activity. Dominant-negative mutants, specific kinase inhibitors, phosphorylation-site mutagenesis (T156A), endocytosis assays in renal epithelial and lung alveolar cells American Journal of Respiratory Cell and Molecular Biology High 16498080
2006 Functional analysis using siRNA knockdown of endogenous μ2 and replacement with wild-type or mutant siRNA-resistant transgenes showed that: mutating the phosphorylation site (T156A), the YXXφ binding site, or the PI(4,5)P2 binding site of α impairs AP-2 function (transferrin uptake); removing the α C-terminal appendage domain or mutating the PI(4,5)P2 binding site of μ2 alone has no apparent effect; no single mutation totally abolishes AP-2 function, indicating functional redundancy among binding sites. Stable transfection of siRNA-resistant wild-type and mutant subunits, siRNA knockdown, transferrin uptake assay Molecular Biology of the Cell High 17035630
2008 AP2M1 (AP50/μ2) mediates clathrin-dependent endocytosis of soybean ferritin in intestinal Caco-2 cells; RNAi knockdown of the μ2 subunit of AP-2 prevents ferritin uptake, demonstrating AP2M1's role in intestinal iron absorption via clathrin-mediated endocytosis. RNAi knockdown of μ2, confocal microscopy, radiolabeled ferritin uptake, pharmacological inhibition of clathrin-mediated endocytosis The Journal of Nutrition High 18356317
2008 The α1b-adrenergic receptor (but not α1a-AR) binds AP50 (AP2M1), and this interaction—together with β-arrestin binding—mediates receptor endocytosis; the α1a-AR fails to bind AP50 and undergoes negligible endocytosis despite some β-arrestin interaction. Co-immunoprecipitation, confocal microscopy, biotinylation internalization assays, RNA interference of β-arrestin Molecular Pharmacology Medium 18523139
2008 In C. elegans, the μ2 homolog APM-2 (encoded by apm-2/dpy-23) is highly expressed in neurons and localizes to synapses; loss of APM-2 mislocalizes clathrin at synapses and reduces synaptic vesicle numbers to ~60% and evoked responses to ~65%, demonstrating that μ2 facilitates but is not essential for synaptic vesicle recycling. Genetic loss-of-function, immunolocalization, electrophysiological recording, electron microscopy of synaptic vesicles The Journal of Cell Biology High 19047463
2009 No single perturbation of μ2 (AP2M1) function—including mutations in the PI(4,5)P2 binding site, YXXφ binding site, or phosphorylation site—prevents restoration of endocytic function at nerve terminals; only introduction of multiple distributed mutations significantly impairs synaptic vesicle endocytosis, indicating a distributed network of interactions supports AP-2 function in SV endocytosis. Quantitative endocytosis assays at hippocampal nerve terminals with systematic μ2 mutagenesis The Journal of Biological Chemistry High 19762466
2009 Phospholipase D1 (PLD1) directly interacts with AP2M1 (μ2) in an auto-regulatory manner dependent on PLD1's own product phosphatidic acid; this interaction facilitates AP-2 membrane recruitment and accelerates EGFR endocytosis kinetics. Co-immunoprecipitation, kinetic endocytosis analysis, dominant-negative and knockdown approaches PLoS ONE Medium 19763255
2012 HCV core protein contains a conserved YXXφ motif that mediates direct binding to AP2M1; this interaction (confirmed by microfluidics affinity analysis, protein-fragment complementation assays, and co-immunoprecipitation) recruits AP2M1 to lipid droplets and is essential for HCV assembly but not RNA replication. Disruption by YXXΦ mutation, AP2M1 silencing, or dominant-negative AP2M1 causes core accumulation on lipid droplets and blocks virion maturation. AAK1 and GAK kinases regulate core–AP2M1 binding and HCV assembly. Microfluidics affinity analysis, protein-fragment complementation, co-immunoprecipitation, siRNA knockdown, dominant-negative overexpression, quantitative confocal immunofluorescence, infectivity assays PLoS Pathogens High 22916011
1988 AP50 (AP2M1) was molecularly cloned from rat brain; the encoded 435-amino-acid protein (MW ~49,612 Da) is highly conserved between rat and bovine brain and is a structural component of the AP-2 assembly protein complex of clathrin-coated vesicles, with no detectable kinase sequence similarity. cDNA cloning, sequencing, and sequence comparison DNA Medium 3148444
1993 AP2M1 (AP50) is phosphorylated in vitro on Thr-156 by a kinase activity co-purifying with AP complexes (identified as AP-1-associated and a soluble ~280 kDa kinase complex); only a single phosphorylation site exists in AP50. In vitro phosphorylation, tryptic peptide mapping, automated Edman degradation, Mono-Q and reverse-phase HPLC, gel filtration The Biochemical Journal High 8257432
1995 The human AP2M1 gene (CLAPM1) was chromosomally mapped to 3q28 by in situ hybridization, establishing its genomic location. Chromosomal in situ hybridization with human genomic clone Genomics Medium 8595912
2003 CD22 (B cell coreceptor) interacts with AP50 (AP2M1) via tyrosine-based internalization motifs in its cytoplasmic domain; Tyr843 is the primary binding site for AP50, with Tyr863 providing a redundant motif sufficient for mAb-mediated internalization and AP-2 complex association. Yeast two-hybrid, co-precipitation of α-adaptin, internalization assays with wild-type and mutant CD22 transfectants Journal of Immunology Medium 12646615
2019 A recurrent de novo missense variant p.Arg170Trp in AP2M1 impairs the conformational activation and thermodynamic entropy of the AP-2 complex, significantly reducing clathrin-mediated endocytosis of transferrin in human cells and in astrocytes from AP-2μ conditional knockout mice, without affecting AP2M1 stability, expression, membrane recruitment, or localization, causing developmental and epileptic encephalopathy. Whole-exome sequencing, molecular dynamics modeling, functional complementation in human cells and mouse astrocytes, transferrin uptake assay American Journal of Human Genetics High 31104773
2020 Multiple viruses (influenza A, Zika, HIV, MERS-CoV, SARS-CoV-2, EV-A71) exploit host AP2M1 via a common YXXφ motif to achieve intracellular trafficking; AP2M1 depletion or YXXφ mutation causes incorrect localization of viral proteins (e.g., failure of IAV nucleoprotein nuclear import, loss of ER localization of ZIKV-NS3). The compound ACA interrupts AP2M1–virus interaction and broadly inhibits viral replication in vitro and in vivo. YXXφ mutagenesis, AP2M1 siRNA depletion, immunofluorescence localization assays, antiviral efficacy assays in vitro and in vivo Science Advances High 32923629
2021 LRRK2 (Parkinson's disease kinase) directly binds and phosphorylates AP2M1 at Thr(156); loss of LRRK2 decreases AP2M1 phosphorylation impairing initial clathrin-coated vesicle (CCV) formation, while overexpression or gain-of-function LRRK2 G2019S inhibits AP2M1 uncoating from CCVs, blocking new CCV cycles. Dysregulated AP2M1 phosphorylation mediates dopaminergic neurodegeneration in a Drosophila PD model, and the effect is brain-tissue-specific. Co-immunoprecipitation, kinase assay, phosphorylation-site analysis, mouse brain/thyroid tissue analysis, Drosophila neurodegeneration model Science Signaling High 34315807
2021 AP2M1 mediates clathrin-dependent endocytosis of CLDN2 (claudin-2) during starvation-induced autophagy; AP2M1 binds CLDN2 via YXXΦ motifs at residues 67–70 and 148–151, and increased AP2M1 phosphorylation upon starvation enhances CLDN2 endocytosis. AP2M1 also interacts with LC3, linking clathrin-mediated endocytosis to autophagosomal degradation of CLDN2, thereby reducing intestinal tight junction permeability. AP2M1 knockout abolishes autophagy-induced CLDN2 degradation. Co-immunoprecipitation, membrane fractionation, pharmacological inhibition, CRISPR/Cas9 knockout, site-directed mutagenesis of YXXφ motifs, in vitro/in vivo/ex vivo validation Autophagy High 34964704
2017 AP2M1 (μ2) mediates clathrin-mediated endocytosis of N-cadherin via two tyrosine-based motifs in N-cadherin's cytoplasmic domain; β-catenin inhibits this endocytosis by masking these motifs, and removal of β-catenin facilitates μ2 binding to N-cadherin, increasing CME and promoting neurite outgrowth without altering steady-state surface N-cadherin levels. Co-immunoprecipitation, site-directed mutagenesis of YXXφ motifs, live-cell endocytosis assays, neurite outgrowth quantification Traffic High 28224728
2021 In C. elegans, dpy-23 (AP2M1 ortholog) mutation reduces TGF-β signaling by upregulating caveolin-1 (cav-1) in the hypodermis; increased CAV-1 leads to decreased TβRI receptor levels and reduced collagen expression. Knockdown of cav-1 restores TGF-β signaling in dpy-23 mutants, placing AP2M1 upstream of caveolin-mediated regulation of TGF-β receptor abundance and ECM production. Suppressor genetic screen, RNA-seq, epistasis analysis, cav-1 RNAi knockdown in C. elegans International Journal of Molecular Sciences Medium 33561975
2022 HPV-16 E7 binds directly to AP2M1 (AP2-μ2) via a YXXφ-like motif (25-YEQL-28) within the LXCXE region; this binding is independent of pRB binding and is facilitated by CKII phosphorylation of serines 31/32. E7–AP2M1 interaction contributes to cellular transformation by inhibiting AP2-mediated EGFR internalization under low-nutrient conditions. Mutagenesis of Y25, co-immunoprecipitation, CKII phosphorylation, EGFR internalization assay, transformation assay mBio High 36255238
2021 In developing cortical neurons, Vangl2 (planar cell polarity protein) interacts with AP2M1 at both its N-terminal and C-terminal Prickle-binding domains; knockdown of AP2M1 in developing cortical neurons reduces dendritic branching similarly to Vangl2 knockdown, indicating AP2M1-mediated membrane internalization is required for normal dendritic morphogenesis. Yeast two-hybrid screen, pull-down assay, shRNA knockdown in cortical neurons, dendritic morphology quantification Genes to Cells Medium 34626136
2024 AP2M1 (μ2) directly interacts with SLC26A4 (Pendrin) in the endolymphatic sac, regulating its plasma membrane abundance via clathrin-mediated endocytosis; structural modeling identified the interaction elements and pharmacological inhibition of CME increases SLC26A4 apical membrane abundance in mitochondria-rich cells. Co-localization, structural modeling validated experimentally, pharmacological inhibition of CME, HA-tagged SLC26A4 abundance assay in vivo and in vitro Science Advances High 39383236
2018 AP2M1 is a target of the cdk4-EZH2 pathway during senescence escape; proteomic analysis identified AP2M1 as involved in receptor endocytosis in this context, and AP2M1 was found to participate in transmission of paracrine signals produced by senescent cells, suggesting it regulates specific receptors involved in control of chemotherapy-induced senescence escape. Quantitative proteomics, siRNA, EZH2 inhibitor treatment, colony emergence assay Cell Death & Disease Low 29415991

Source papers

Stage 0 corpus · 130 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2020 A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature 3411 32353859
2005 Towards a proteome-scale map of the human protein-protein interaction network. Nature 2090 16189514
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2008 Identification of host proteins required for HIV infection through a functional genomic screen. Science (New York, N.Y.) 1165 18187620
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2012 A mega-analysis of genome-wide association studies for major depressive disorder. Molecular psychiatry 846 22472876
1995 Interaction of tyrosine-based sorting signals with clathrin-associated proteins. Science (New York, N.Y.) 843 7569928
1991 Serine phosphorylation-independent downregulation of cell-surface CD4 by nef. Nature 716 2014052
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2010 Plasma membrane contributes to the formation of pre-autophagosomal structures. Nature cell biology 704 20639872
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2006 A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. Cell 610 16713569
2008 Large-scale proteomics and phosphoproteomics of urinary exosomes. Journal of the American Society of Nephrology : JASN 607 19056867
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
2020 Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms. Science (New York, N.Y.) 564 33060197
2003 Clathrin-mediated endocytosis in AP-2-depleted cells. The Journal of cell biology 563 12952941
2003 A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nature biotechnology 558 12577067
2021 Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature 532 33845483
1998 A structural explanation for the recognition of tyrosine-based endocytotic signals. Science (New York, N.Y.) 504 9812899
2002 Molecular architecture and functional model of the endocytic AP2 complex. Cell 495 12086608
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