Literature DB >> 33415776

Regulation and function of the palmitoyl-acyltransferase ZDHHC5.

Keith T Woodley1,2, Mark O Collins1.   

Abstract

Protein palmitoylation (S-acylation) has emerged as an important player in a range of cellular processes, and as a result, the palmitoyl-acyltransferase (PAT) enzymes which mediate this modification have entered into the spotlight. Palmitoyltransferase ZDHHC5 (ZDHHC5) is among the more unique members of the PAT family as it is mainly localised to the plasma membrane and contains an extended cytoplasmic domain with several regulatory features. ZDHHC5 plays a vital role in a wide range of processes in different cell types. In this review, we offer a summary of the functions of ZDHHC5 in synaptic plasticity, cardiac function, cell adhesion and fatty acid uptake, among other processes. We also explore recent work has revealed several mechanisms to control the activity, localisation and function of ZDHHC5.
© 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

Entities:  

Keywords:  S-acylation; ZDHHC5; membrane; palmitoylation

Mesh:

Substances:

Year:  2021        PMID: 33415776     DOI: 10.1111/febs.15709

Source DB:  PubMed          Journal:  FEBS J        ISSN: 1742-464X            Impact factor:   5.542


  2 in total

1.  The interactions of ZDHHC5/GOLGA7 with SARS-CoV-2 spike (S) protein and their effects on S protein's subcellular localization, palmitoylation and pseudovirus entry.

Authors:  Xiao-Tao Zeng; Xiao-Xi Yu; Wei Cheng
Journal:  Virol J       Date:  2021-12-27       Impact factor: 4.099

2.  Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo.

Authors:  Gonzalo P Solis; Arghavan Kazemzadeh; Laurence Abrami; Jana Valnohova; Cecilia Alvarez; F Gisou van der Goot; Vladimir L Katanaev
Journal:  Nat Commun       Date:  2022-04-19       Impact factor: 17.694

  2 in total

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