The E3 ligase Poe promotes Pericentrin degradation-Reference-Cited by-同舟云学术

The E3 ligase Poe promotes Pericentrin degradation

Published:2023-08-01 Issue:9 Volume:34 Page:
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Galletta Brian J.¹,Varadarajan Ramya¹,Fagerstrom Carey J.¹,Yang Bing²,Haase Karen Plevock¹,McJunkin Katherine²,Rusan Nasser M.¹

Affiliation:

1. Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, and

2. Laboratory of Cellular and Developmental Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892

Abstract

In this study, we demonstrate that Pericentrin-like protein (PLP) is regulated by posttranslational protein degradation in the germ line. In a screen for regulators of PLP positioning along spermatocyte centriole, we identified proteins critical for this regulation, including the E3 ligase Poe. Our data indicate that PLP is under multiple levels of regulation to ensure the proper timing of its availability during centriole elongation.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

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1. Association studies and gene expression analyses of the DISC1-interacting molecules, pericentrin 2 (PCNT2) and DISC1-binding zinc finger protein (DBZ), with schizophrenia and with bipolar disorder

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3. Cell-cycle-regulated expression of STIL controls centriole number in human cells

4. Ubiquitin signaling in the control of centriole duplication

5. The ubiquitin ligase FBXW7 targets the centriolar assembly protein HsSAS-6 for degradation and thereby regulates centriole duplication

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