86 0

The role of deubiquitinating enzymes in spermatogenesis

Title
The role of deubiquitinating enzymes in spermatogenesis
Author
Ramakrishna Suresh
Keywords
Acrosome; Gonocytes; Male infertility; Nucleosome; Proteasome; Protein degradation; Spermiogenesis; Ubiquitin
Issue Date
2015-12
Publisher
SPRINGER BASEL AG
Citation
CELLULAR AND MOLECULAR LIFE SCIENCES, v. 72, NO 24, Page. 4711-4720
Abstract
Spermatogenesis is a complex process through which spermatogonial stem cells undergo mitosis, meiosis, and cell differentiation to generate mature spermatozoa. During this process, male germ cells experience several translational modifications. One of the major post-translational modifications in eukaryotes is the ubiquitination of proteins, which targets proteins for degradation; this enables control of the expression of enzymes and structural proteins during spermatogenesis. It has become apparent that ubiquitination plays a key role in regulating every stage of spermatogenesis starting from gonocytes to differentiated spermatids. It is understood that, where there is ubiquitination, deubiquitination by deubiquitinating enzymes (DUBs) also exists to counterbalance the ubiquitination process in a reversible manner. Normal spermatogenesis is dependent on the balanced actions of ubiquitination and deubiquitination. This review highlights the current knowledge of the role of DUBs and their essential regulatory contribution to spermatogenesis, especially during progression into meiotic phase, acrosome biogenesis, quality sperm production, and apoptosis of germ cells.
URI
https://link.springer.com/article/10.1007%2Fs00018-015-2030-zhttp://hdl.handle.net/20.500.11754/30253
ISSN
1420-682X; 1420-9071
DOI
10.1007/s00018-015-2030-z
Appears in Collections:
GRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S](의생명공학전문대학원) > ETC
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE