Noncanonical functions of the serine‐arginine‐rich splicing factor (SR) family of proteins in development and disease

Bioessays 43 (4):2000242 (2021)
  Copy   BIBTEX

Abstract

Members of the serine/arginine (SR)‐rich protein family of splicing factors play versatile roles in RNA processing steps and are often essential for normal development. Dynamic changes in RNA processing and turnover allow fast cellular adaptions to a changing microenvironment and thereby closely cooperate with transcription factor networks that establish cell identity within tissues. SR proteins play fundamental roles in the processing of pre‐mRNAs by regulating constitutive and alternative splicing. More recently, SR proteins have also been implicated in other aspects of RNA metabolism such as mRNA stability, transport and translation. The‐ emerging noncanonical functions highlight the multifaceted functions of these SR proteins and identify them as important coordinators of gene expression programmes. Accordingly, most SR proteins are essential for normal cell function and their misregulation contributes to human diseases such as cancer.

Links

PhilArchive



    Upload a copy of this work     Papers currently archived: 92,227

External links

Setup an account with your affiliations in order to access resources via your University's proxy server

Through your library

Similar books and articles

Schizophrenia in adolescents and the family system.Waldemar Świętochowski - 2011 - Polish Psychological Bulletin 42 (1):5-10.
Covid 19 pandemic: Impact on masses and prevention knowhow. Namita, Chitra Singh & Vivek Kumar - 2020 - International Journal of Medical and Health Research 6 (9):6-9.
Alternative Splicing, the Gene Concept, and Evolution.Stephen Downes - 2004 - History and Philosophy of the Life Sciences 26 (1):91 - 104.

Analytics

Added to PP
2021-02-09

Downloads
4 (#1,628,455)

6 months
2 (#1,206,802)

Historical graph of downloads
How can I increase my downloads?

Citations of this work

No citations found.

Add more citations

References found in this work

No references found.

Add more references