Post-Translational Modifications and RNA-Binding Proteins

被引:26
|
作者
Lovci, Michael T. [1 ]
Bengtson, Mario H. [2 ]
Massirer, Katlin B. [1 ]
机构
[1] Univ Estadual Campinas, CBMEG UNICAMP, Ctr Mol Biol & Genet Engn, Av Candido Rondon 400, BR-13083875 Sao Paulo, Brazil
[2] Univ Estadual Campinas, Inst Biol, Dept Biochem & Tissue Biol, Av Monteiro Lobato 255, BR-13083970 Sao Paulo, Brazil
关键词
RNA-binding proteins; Post-translational modifications; SUMOylation; Ubiquitination; Phosphorylation; PRE-MESSENGER-RNA; MENTAL-RETARDATION PROTEIN; XENOPUS OOCYTE MATURATION; SPLICING REPRESSOR SRP38; CARBOXY-TERMINAL DOMAIN; POLYMERASE-II; SR PROTEIN; DNA-DAMAGE; CYTOPLASMIC POLYADENYLATION; TYROSINE PHOSPHORYLATION;
D O I
10.1007/978-3-319-29073-7_12
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
RNA-binding proteins affect cellular metabolic programs through development and in response to cellular stimuli. Though much work has been done to elucidate the roles of a handful of RNA-binding proteins and their effect on RNA metabolism, the progress of studies to understand the effects of post-translational modifications of this class of proteins is far from complete. This chapter summarizes the work that has been done to identify the consequence of post-translational modifications to some RNA-binding proteins. The effects of these modifications have been shown to increase the panoply of functions that a given RNA-binding protein can assume. We will survey the experimental methods that are used to identify the presence of several protein modifications and methods that attempt to discern the consequence of these modifications.
引用
收藏
页码:297 / 317
页数:21
相关论文
共 50 条
  • [31] POST-TRANSLATIONAL MODIFICATIONS OF MITOCHONDRIAL OUTER MEMBRANE PROTEINS
    Distler, Anne M.
    Kerner, Janos
    Lee, Kwangwon
    Hoppel, Charles L.
    METHODS IN ENZYMOLOGY, VOL 457: MITOCHONDRIAL FUNCTION, PARTB MITOCHONDRIAL PROTEIN KINASES, PROTEIN PHOSPHATASES AND MITOCHONDRIAL DISEASES, 2009, 457 : 97 - 115
  • [32] Post-translational modifications of proteins in antiphospholipid antibody syndrome
    Buttari, Brigitta
    Profumo, Elisabetta
    Capozzi, Antonella
    Saso, Luciano
    Sorice, Maurizio
    Rigano, Rachele
    CRITICAL REVIEWS IN CLINICAL LABORATORY SCIENCES, 2019, 56 (08) : 511 - 525
  • [33] Impact of post-translational modifications of proteins on the inflammatory process
    Ito, K.
    BIOCHEMICAL SOCIETY TRANSACTIONS, 2007, 35 : 281 - 283
  • [34] The Ras superfamilies: regulatory proteins and post-translational modifications
    Evans, Tony
    Hart, Matthew J.
    Cerione, Richard A.
    CURRENT OPINION IN CELL BIOLOGY, 1991, 3 (02) : 185 - 191
  • [35] Advances in post-translational modifications of proteins and cancer immunotherapy
    Li, Yanqing
    Zhang, Runfang
    Hei, Hu
    FRONTIERS IN IMMUNOLOGY, 2023, 14
  • [36] Is there a code embedded in proteins that is based on post-translational modifications?
    Sims, Robert J., III
    Reinberg, Danny
    NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2008, 9 (10) : 815 - 820
  • [37] Post-translational modifications of host proteins in pathogen defense
    Xavier, Ramnik
    FASEB JOURNAL, 2014, 28 (01):
  • [38] Post-translational modifications of coronavirus proteins: roles and function
    Fung, To Sing
    Liu, Ding Xiang
    FUTURE VIROLOGY, 2018, 13 (06) : 405 - 430
  • [39] Post-translational modifications of recombinant proteins: Significance for biopharmaceuticals
    Jenkins, Nigel
    Murphy, Lisa
    Tyther, Ray
    MOLECULAR BIOTECHNOLOGY, 2008, 39 (02) : 113 - 118
  • [40] Post-translational Modifications of Recombinant Proteins: Significance for Biopharmaceuticals
    Nigel Jenkins
    Lisa Murphy
    Ray Tyther
    Molecular Biotechnology, 2008, 39 : 113 - 118