Signal-Seeker™: cytoskeleton protein  PTMs

 

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Actin Post-Translational Modifications

Introduction

Post-translational modifications (PTMs) are highly dynamic and often reversible processes where a protein’s functional properties are altered by addition of a chemical group or another protein to its amino acid residues.  As a major cytoskeletal protein with roles in cell development, growth, motility, and intracellular trafficking, actin is a major substrate for PTMs.  Actin can undergo at least 17 PTMs that include ADP-ribosylation, arginylation, dimethylation, phosphorylation, oxidation, nitration, O-GlcNAcylation, ubiquitination, SUMOylation, acetylation, carbonylation, isaspartylation, transglutamination, malonylation, glutathionylation, nitrosylation, and crosslinking/isopeptide bonding .  Click here to see a summary of what is currently known about many of these actin PTMs.

 

Tubulin Post-Translational Modifications

Introduction

Post-translational modifications (PTMs) are highly dynamic and often reversible processes where a protein’s functional properties are altered by addition of a chemical group or another protein to its amino acid residues. As a major cytoskeletal protein with roles in cell development, growth, motility, and intracellular trafficking, tubulin and microtubules (MTs) are a major substrate for PTMs. Tubulin PTMs usually occur post-polymerization and preferentially on the a/b tubulin heterodimers of stable (vs dynamic) MTs1-3. Here, we review the current understanding of tubulin PTMs that include tyrosination/detyrosination, Δ2-tubulin formation, acetylation, phosphorylation, ubiquitination, glutamylation, and glycylation. Click here to see a brief background on the modifications, modifying enzymes (if known), and the potential function(s) of the tubulin PTM.