World Library  
Flag as Inappropriate
Email this Article

Polyglutamylation

Article Id: WHEBN0008126986
Reproduction Date:

Title: Polyglutamylation  
Author: World Heritage Encyclopedia
Language: English
Subject: Detyrosination, SUMO protein, Protein biosynthesis, Phosphorylation, Proteolysis
Collection:
Publisher: World Heritage Encyclopedia
Publication
Date:
 

Polyglutamylation

Polyglutamylation is a form of reversible posttranslational modification of glutamate residues seen for example in alpha and beta tubulins, nucleosome assembly proteins NAP1 and NAP2. The γ-carboxy group of glutamate may form peptide-like bond with the amino group of a free glutamate whose α-carboxy group can now be extended into a polyglutamate chain.[1] The glutamylation is done by the enzyme glutamylase and removed by deglutamylase.

Polyglutamylation of chain length of up to six occurs in certain glutamate residues near the C terminus of most major forms of tubulins. These residues, though themselves not involved in direct binding, cause conformational shifts that regulate binding of microtubule associated proteins (MAP and Tau) and motors.[2]

External links

  • The role of tubulin polymodifications in microtubule functions

References

  1. ^ "Polyglutamylation: mechanism". 
  2. ^ Boucher D, Larcher JC, Gros F, Denoulet P (October 1994). "Polyglutamylation of tubulin as a progressive regulator of in vitro interactions between the microtubule-associated protein Tau and tubulin". Biochemistry 33 (41): 12471–7.  
This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and USA.gov, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for USA.gov and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
 
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
 
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.
 



Copyright © World Library Foundation. All rights reserved. eBooks from Hawaii eBook Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.