| 2002 |
PCM-1 localizes to centriolar satellite granules and is required for microtubule- and dynactin-dependent recruitment of centrin, pericentrin, and ninein to the centrosome. Inhibition or depletion of PCM-1 (via antibody microinjection, dominant-negative overexpression, or siRNA) disrupts radial microtubule organization without affecting microtubule nucleation. Loss of centrin or ninein also disrupts microtubule organization, placing PCM-1 upstream of these proteins in centrosome maturation. |
Antibody microinjection, dominant-negative overexpression, siRNA knockdown, immunofluorescence microscopy |
The Journal of cell biology |
High |
12403812
|
| 1994 |
PCM-1 is a 228-kDa centrosomal protein that dissociates from the centrosome late in G2 and remains dispersed during mitosis, then re-associates with centrosomes in G1 daughter cells, demonstrating cell-cycle-dependent centrosome association. |
Immunofluorescence microscopy with anti-recombinant PCM-1 antibodies across cell cycle stages |
The Journal of cell biology |
Medium |
8120099
|
| 2003 |
PCM-1 self-aggregates through two distinct regions in its N-terminal domain to form granules (centriolar satellites), and this self-aggregation is regulated in a cell-cycle-dependent manner (disassembly during mitosis, reassembly in interphase). PCM-1 granules are distinct from pericentrin-containing granules but frequently associate with them. |
Overexpression of deletion mutants, immunofluorescence microscopy, co-localization studies |
Journal of cell science |
Medium |
12571289
|
| 2001 |
PCM-1 and pericentrin-B coimmunoprecipitate, indicating they form a functional complex. The association of both proteins with salt-stripped centrosomes requires intact microtubules. Immunodepletion of neither PCM-1 nor pericentrin-B inhibited microtubule nucleation from salt-stripped centrosomes. |
Coimmunoprecipitation, immunodepletion, microtubule nucleation assay, microtubule depolymerization |
Journal of cell science |
Medium |
11171385
|
| 2005 |
PCM-1-containing centriolar satellites are required for centrosomal recruitment of Nek2 kinase and its substrate C-Nap1. Nek2 exists in dynamic cytoplasmic particles that partially colocalize with PCM-1 satellites. Depletion of PCM-1 by siRNA interferes with centrosomal recruitment of Nek2. |
siRNA knockdown of PCM-1, FRAP, immunofluorescence co-localization, co-sedimentation |
Molecular biology of the cell |
Medium |
15659651
|
| 2008 |
CEP290 binds PCM-1 and localizes to centriolar satellites in a PCM-1- and microtubule-dependent manner. Depletion of CEP290 disrupts PCM-1 distribution and protein complex formation. Both CEP290 and PCM-1 are required for ciliogenesis and ciliary targeting of Rab8. |
Coimmunoprecipitation, siRNA knockdown, immunofluorescence microscopy |
Human molecular genetics |
Medium |
18772192
|
| 2008 |
PCM1 forms a complex with DISC1 and BBS4 through discrete binding domains in each protein. DISC1 and BBS4 are synergistically required for targeting PCM1 and cargo proteins (e.g., ninein) to the centrosome. Suppression of PCM1 in the developing cerebral cortex causes neuronal migration defects phenocopied by DISC1 or BBS4 suppression. |
Coimmunoprecipitation, immunofluorescence, RNAi in vivo (in utero electroporation) |
Archives of general psychiatry |
High |
18762586
|
| 2010 |
Hook3 is recruited to pericentriolar satellites through direct interaction with PCM1. Disruption of the Hook3-PCM1 interaction in vivo impairs interkinetic nuclear migration of embryonic neural progenitors, leading to overproduction of neurons and premature depletion of the neural progenitor pool. |
Coimmunoprecipitation, in utero electroporation (RNAi), live imaging |
Neuron |
High |
20152126
|
| 2011 |
Huntingtin (HTT) regulates retrograde trafficking of PCM1 to the centrosome through HAP1. Loss of Htt impairs PCM1 retrograde trafficking and reduces primary cilia formation. Pathogenic polyQ expansion causes centrosomal accumulation of PCM1 and abnormally long primary cilia. HTT-HAP1-PCM1 defines a pathway for centrosome protein trafficking and ciliogenesis. |
Conditional knockout mice, coimmunoprecipitation, immunofluorescence, live imaging, cilia measurement |
The Journal of clinical investigation |
High |
21985783
|
| 2013 |
PCM1 acts upstream of Plk1 and recruits Plk1 to the pericentriolar matrix in a dynein-dynactin-dependent manner to promote primary cilia disassembly before mitotic entry. PCM1-Plk1 interaction is phosphorylation-dependent with CDK1 acting as the priming kinase. Plk1 then activates HDAC6 to deacetylate and resorb cilia. shRNA depletion of PCM1 disrupts pericentriolar accumulation of Plk1. |
shRNA knockdown, coimmunoprecipitation, phosphorylation assays, immunofluorescence microscopy |
Journal of cell science |
High |
23345402
|
| 2016 |
PCM1 is essential for tethering the E3 ubiquitin ligase Mindbomb1 (Mib1) to centriolar satellites. In the absence of PCM1, Mib1 destabilizes Talpid3 through poly-ubiquitylation and suppresses ciliogenesis. Loss of PCM1 blocks recruitment of Rab8-associated ciliary vesicles to centrioles; this block can be reversed by inactivating Mib1. An amino-terminal domain of PCM1 restores ciliogenesis and satellite localization of certain proteins. |
Gene deletion (PCM1 null human cells), coimmunoprecipitation, ubiquitylation assay, immunofluorescence, domain mapping |
eLife |
High |
27146717
|
| 2016 |
Plk4 phosphorylates PCM1 at the conserved S372 residue. This phosphorylation occurs during G1 phase and is required for PCM1 dimerization and interaction with other satellite components, as well as centriolar satellite integrity and ciliogenesis. Non-phosphorylatable S372A mutant recapitulates Plk4 depletion phenotypes; phosphomimetic mutant partially rescues dispersed satellites and ciliogenesis in PCM1-depleted cells. |
Kinase assay (Plk4 phosphorylation of PCM1), phosphomutant/phosphomimetic rescue experiments, coimmunoprecipitation, immunofluorescence |
EMBO reports |
High |
26755742
|
| 2019 |
SNX17 recruits the deubiquitinating enzyme USP9X to antagonize MIB1-mediated ubiquitination and proteasomal degradation of PCM1 during serum-starvation-induced ciliogenesis. SNX17 deficiency leads to enhanced degradation of USP9X and PCM1 and disrupts ciliogenesis. This SNX17/USP9X pathway is dispensable for PCM1 homeostasis in serum-containing media. |
Co-immunoprecipitation, siRNA knockdown, ubiquitination assay, immunofluorescence, ciliogenesis assay |
Cells |
Medium |
31671755
|
| 2019 |
Zika virus infection increases MIB1 (E3 ubiquitin ligase) levels, leading to MIB1-mediated ubiquitination and proteasomal degradation of PCM1, causing dispersion of PCM1-containing centriolar satellite granules. MIB1 knockout cells are resistant to ZIKV-induced PCM1 degradation and granule dispersion. Proteasome inhibitor MG132 prevents PCM1 loss. |
Viral infection, MIB1 knockout cells, proteasome inhibition (MG132), immunofluorescence, Western blot |
The Journal of biological chemistry |
Medium |
31666336
|
| 2020 |
Trichoplein (TCHP) localizes to centriolar satellites, binds PCM1, and stabilizes it. Loss of TCHP leads to delocalization and proteasome-dependent degradation of PCM1, and further results in degradation of PCM1's binding partner GABARAP, impairing autophagic flux in endothelial cells. |
Coimmunoprecipitation, siRNA knockdown, immunofluorescence, autophagic flux assay, Tchp knockout mice |
EMBO reports |
Medium |
32337819
|
| 2020 |
PCM1 ablation in mice leads to progressive ciliary integrity defects, reduced available dopamine D2 receptor (D2R) levels, and behavioral abnormalities. Immunoprecipitation shows an association between Pcm1 and D2Rs. Antipsychotic drugs fail to rescue adult behavioral defects in Pcm1-null mice. |
Mouse knockout, immunoprecipitation, immunofluorescence, behavioral testing, RNAseq |
Nature communications |
Medium |
33214552
|
| 2013 |
PCM1-JAK2 fusion protein signals through STAT5 to upregulate SOCS2 and SOCS3. Lentiviral knockdown of PCM1-JAK2 inhibited these top upregulated genes. Treatment with a selective JAK2 inhibitor confirmed that JAK2 is the active signaling moiety. PCM1-JAK2 requires pSTAT5 for its downstream signaling. |
Lentiviral shRNA knockdown, JAK2 inhibitor treatment, gene expression profiling |
PloS one |
Medium |
23372669
|
| 2024 |
Necrosulfonamide (NSA) causes oxidation and aggregation of PCM1 independently of MLKL, identifying PCM1 as a redox sensor protein. NSA-mediated ROS production disrupts ciliogenesis and leads to accumulation of autophagy markers; deletion of PCM1 partially alleviates NSA-induced autophagy accumulation. |
PCM1 deletion (CRISPR), ROS measurement, immunofluorescence, ciliogenesis assay, autophagy flux assay |
iScience |
Medium |
38600973
|
| 2025 |
PCM1 binds centrosomal proteins and governs their translocation via intra-manchette transport during spermiogenesis. Pcm1 knockout mice exhibit disorganized manchette, head-tail coupling apparatus defects, defective flagellogenesis, and male infertility. Loss of PCM1 in sperm also causes severe retardation of embryo development that cannot be overcome by ICSI. |
Mouse knockout (Pcm1 KO), immunofluorescence, co-immunoprecipitation, electron microscopy, ICSI |
Communications biology |
Medium |
40481240
|
| 2025 |
Pcm1 is asymmetrically associated with Cep83 (a mother centrosome marker) in radial glia progenitors (RGPs) and is detected on Notch ligand-containing endosomes in a complex with Par-3 and dynein. Loss of pcm1 disrupts endosome dynamics (impairing Rab5b-to-Rab11a transition) and reduces Par-3/dynein macromolecular complex assembly on recycling endosomes, increasing neuronal differentiation at the expense of RGP self-renewal. PARD3-PCM1-CEP83-RAB11 associations are conserved in human cortical brain organoids. |
In vivo time-lapse imaging, expansion microscopy, coimmunoprecipitation, loss-of-function (pcm1 KO/KD), clonal analysis, brain organoids |
Nature communications |
High |
41315244
|
| 2025 |
Centriolar satellites (CS) assemble via a hierarchical pathway in which PCM1 scaffold formation (through intrinsic multimerization modulated by the cytoskeleton) precedes regulated client recruitment. PCM1 and its clients occupy distinct subdomains with different compositions and dynamics. Perturbing PCM1 multimerization impairs ciliary signaling. |
Cellular and in vitro CS biogenesis assays, high-resolution imaging, spatiotemporal quantification, PCM1 multimerization mutants |
bioRxivpreprint |
Medium |
bio_10.1101_2025.07.27.666075
|
| 2025 |
CCHCR1 interacts with PCM1 to determine its centrosomal localization. CCHCR1 also interacts with OFD1 (via its C-terminal coiled-coil domain) and recruits P-body proteins (EDC4) to the centrosome (via its N-terminal coiled-coil domain). Depletion of CCHCR1 impairs ciliogenesis, placing CCHCR1 in a PCM1/OFD1-dependent pathway for cilia development. |
BioID/mass spectrometry, coimmunoprecipitation, GST pulldown, AB-FRET, siRNA knockdown, CRISPR KO, immunofluorescence |
Cellular & molecular biology letters |
Medium |
40883668
|
| 2005 |
The PCM1-JAK2 fusion gene created by t(8;9)(p22;p24) encodes a chimeric protein retaining coiled-coil domains from PCM1 and the entire tyrosine kinase domain of JAK2. This fusion constitutively activates JAK2 kinase activity and drives hematologic malignancy. Reciprocal JAK2-PCM1 mRNA was not detected. |
RACE-PCR, RT-PCR, FISH, sequencing of chimeric mRNA |
Cancer research |
Medium |
15805263
|