POC1B

Last update 08 May 2025

Basic Info

Synonyms

FLJ14923, Pix1, POC1 centriolar protein B

+ [6]

Introduction

Plays an important role in centriole assembly and/or stability and ciliogenesis (PubMed:20008567, PubMed:32060285). Involved in early steps of centriole duplication, as well as in the later steps of centriole length control (PubMed:19109428). Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation (PubMed:32060285). Required for primary cilia formation, ciliary length and also cell proliferation (PubMed:23015594). Required for retinal integrity (PubMed:25044745). Acts as a positive regulator of centriole elongation (PubMed:37934472).

100 Clinical Results associated with POC1B

100 Translational Medicine associated with POC1B

0 Patents (Medical) associated with POC1B

Literatures (Medical) associated with POC1B

01 Jul 2025·Human Genetics and Genomics Advances

Severe Joubert syndrome in family with homozygous POC1B p.Arg106Pro variant is due to a co-inherited deep-intronic mutation in the neighboring CEP290 gene

Article

Author: Beck, Bodo B ; Reusch, Björn ; Bolz, Hanno J ; Habbig, Sandra ; Betz, Christian ; Langmann, Thomas

"En bloc" inheritance of point mutations in adjacent genes has rarely been described. We have previously reported a family with severe, mostly early-lethal Joubert syndrome (JBTS) with early-onset severe retinal dystrophy (EOSRD) and polycystic kidney disease (PKD), which at that time had been attributed to a homozygous pathogenic missense variant, p.Arg106Pro (c.317G>C), in the ciliary POC1B gene. Because this and other POC1B variants were, in subsequent studies, only reported in patients with non-syndromic childhood or early-adult-onset macular dystrophy, we have now reassessed our index patient by long-read high-fidelity (HiFi) whole-genome sequencing (LR-WGS). We identified a homozygous deep-intronic variant, c.2818-657T>G, in CEP290, a JBTS/Meckel syndrome-associated gene on chromosome 12q21, only 1.28 Mb from the N terminus of POC1B. cDNA analysis revealed aberrant splicing with the frame-shifting inclusion of 37 bp from CEP290 intron 25, predicting the loss of CEP290 function. EOSRD and PKD can fully be ascribed to this CEP290 variant, whose effect outshines the "background" non-syndromic POC1B retinopathy and co-segregates with the severe syndromic phenotype. Our novel findings in this family no longer justify POC1B as a JBTS gene. This co-inheritance of two ciliopathies, with the clinically decisive variant hidden deep in an intron, exemplifies the importance of WGS for achieving the complete diagnosis in challenging cases.

01 Jun 2025·Modern Pathology

Prostate Ductal Adenocarcinoma Revisited: Clinicopathological and Genomic Characterization Identifies Heterogenous Group of Diseases with Implications for Patient Management

Article

Author: Shah, Rajal B ; Cai, Qi ; Meng, Xiaosong ; Sun, Jing ; Mohanty, Sambit K ; Khanshour, Anas M ; Gagan, Jeffrey ; Aggarwal, Aditi ; Bhanvadia, Raj ; Xu, Jing

Prostate ductal adenocarcinoma (PDA) is an aggressive subtype of prostate adenocarcinoma (PA). It can be found either in the peripheral zone, typically associated with acinar PA, or centrally in or around the verumontanum as a urethral polyp. Whether centrally occurring PDAs are biologically and genetically different compared with peripheral PDA remains unknown. Thirty-five PDAs diagnosed on resection specimens were categorized into 3 groups based on PDA location (central [urethra] involvement only [PDA-C], both central and peripheral involvement [PDA-C&P], peripheral involvement only [PDA-P]) and analyzed for clinicopathological, genomic characteristics, and outcomes. Targeted next-generation DNA and RNA sequencing with full exon coverage of 1425 cancer-related genes was performed on 2 PDA-C, 8 PDA-C&P, and 12 PDA-P with a grossly dissectible population of viable PDA. In 11 PDA-P, the same patients' ductal and associated acinar components were sequenced separately. Of 35 PDAs, 2 (6%), 11 (31%), and 22 (63%) were PDA-C, PDA-C&P, and PDA-P, respectively. PDA-C&P compared with PDA-P presented with larger tumor size (median 45 mm vs 25 mm), % ductal component (100% vs 30%), ≥ pT3 disease (100% vs 64%), visceral metastasis (36% vs 0%), and cancer-specific mortality (27% vs 0%) (P < .05) and enrichment for at least 1 DNA damage and repair (DDR)-related gene alterations (BRCA2, ATM, CDK12, ERCC2) (63% vs 8%), and PI3K pathway alterations (37% vs none). PDA-Ps were enriched in FOXA1 alterations compared with PDA-C&P (75% vs 25%) including 5 (56%) having FOXA1 mutation in only ductal components. TMPRSS2::ERG fusion was present in only 1 patient with PDA-P in both ductal and acinar components. One patient with PDA-C and 3 with PDA-C&P exhibited novel gene fusion ACPP::FGFR2 and NF1::ADAP, FGFR2::POC1B, and RB1:TTTY3, respectively. In 2 patients with PDA-C, PDA was eradicated in transurethral resection with no residual disease in follow-up radical prostatectomy. PDA-C lacked alterations in DDR genes. Our findings suggest that PDAs are clinically and genetically heterogeneous diseases. Understanding the heterogeneity of PDA is critically important in determining its biological potential and facilitating optimal patient management.

01 May 2025·Journal of Proteomics

Comparative proteomics and phosphoproteomics analysis reveals differential sperm motility in Mediterranean buffalo semen

Article

Author: Shi, Deshun ; Xue, Qingsong ; Sun, Le ; Xu, Tairan ; Huang, Shihai ; Luo, Xi ; Ren, Xuan ; Yang, Ting ; Li, Xiangping

High motility spermatozoa are good for cryopreservation and artificial insemination (AI) of mammalian semen. In this study, normal motility (NM) and low motility (LM) Mediterranean buffalo spermatozoa were compared using quantitative proteomics and phosphoproteomics techniques to screen for important proteins and phosphorylated proteins related to the motility of spermatozoa and to identify candidate protein molecular markers related to the quality of Mediterranean buffalo semen. Proteomics results identified 2550 proteins, with 119 proteins upregulated and 146 proteins downregulated in the LM spermatozoa versus the NM spermatozoa. The differentially abundant proteins were mainly involved in carbohydrate metabolism, glycolysis/gluconeogenesis, and tricarboxylic acid cycles. The phosphoproteomics analysis revealed 412 proteins, 1228 phosphorylated peptides, and 1465 phosphorylation modification sites. Compared to the NM group, 119 peptides were downregulated in the LM group, corresponding to 98 proteins, and 84 phosphorylated peptides were upregulated in the white matter, corresponding to 61 proteins. Differentially phosphorylated proteins were primarily involved in spermatogenesis, flagellate sperm motility, and glycolysis/gluconeogenesis. The combined proteomics and phosphoproteomics results identified the common proteins HMGB4, POC1B, PKM, LDHA, TBC1D21, and CBY2, whose main roles were related to spermatogenesis, sperm flagellar structure, and energy metabolism, which can be used as potential markers of Mediterranean buffalo sperm quality.

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POC1B

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