Lysine post-translational modifications and the cytoskeleton

Wendy D. Zencheck, Hui Xiao, Louis M. Weiss

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein-protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.

Original languageEnglish (US)
Pages (from-to)135-145
Number of pages11
JournalEssays in Biochemistry
Volume52
Issue number1
DOIs
StatePublished - 2012

Fingerprint

Post Translational Protein Processing
Cytoskeleton
Lysine
Proteins
Eukaryota
Actin Cytoskeleton
Sumoylation
Pseudopodia
Cytoskeletal Proteins
Intermediate Filaments
Flagella
Cilia
Ubiquitination
Acetylation
Regulator Genes
Microtubules
Proteolysis
Accessories
Cell Movement
Processing

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Lysine post-translational modifications and the cytoskeleton. / Zencheck, Wendy D.; Xiao, Hui; Weiss, Louis M.

In: Essays in Biochemistry, Vol. 52, No. 1, 2012, p. 135-145.

Research output: Contribution to journalArticle

Zencheck, Wendy D. ; Xiao, Hui ; Weiss, Louis M. / Lysine post-translational modifications and the cytoskeleton. In: Essays in Biochemistry. 2012 ; Vol. 52, No. 1. pp. 135-145.
@article{89cea8593914489a9f4d9b211835e5cf,
title = "Lysine post-translational modifications and the cytoskeleton",
abstract = "PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein-protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.",
author = "Zencheck, {Wendy D.} and Hui Xiao and Weiss, {Louis M.}",
year = "2012",
doi = "10.1042/BSE0520135",
language = "English (US)",
volume = "52",
pages = "135--145",
journal = "Essays in Biochemistry",
issn = "0071-1365",
publisher = "Portland Press Ltd.",
number = "1",

}

TY - JOUR

T1 - Lysine post-translational modifications and the cytoskeleton

AU - Zencheck, Wendy D.

AU - Xiao, Hui

AU - Weiss, Louis M.

PY - 2012

Y1 - 2012

N2 - PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein-protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.

AB - PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein-protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.

UR - http://www.scopus.com/inward/record.url?scp=84867611373&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84867611373&partnerID=8YFLogxK

U2 - 10.1042/BSE0520135

DO - 10.1042/BSE0520135

M3 - Article

C2 - 22708568

AN - SCOPUS:84867611373

VL - 52

SP - 135

EP - 145

JO - Essays in Biochemistry

JF - Essays in Biochemistry

SN - 0071-1365

IS - 1

ER -