Cytosolic carboxypeptidase 5 removes α- And γ-linked glutamates from tubulin

Iryna Berezniuk; Peter J. Lyons; Juan J. Sironi; Hui Xiao; Mitsutoshi Setou; Ruth H. Angeletti; Koji Ikegami; Lloyd D. Fricker

doi:10.1074/jbc.M113.497917

Cytosolic carboxypeptidase 5 removes α- And γ-linked glutamates from tubulin

Iryna Berezniuk, Peter J. Lyons, Juan J. Sironi, Hui Xiao, Mitsutoshi Setou, Ruth H. Angeletti, Koji Ikegami, Lloyd D. Fricker

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

Background: Cytosolic carboxypeptidase 5 (CCP5) was proposed to selectively cleave γ-linked glutamate from tubulin side chains, but not α-linked glutamates. Results: Purified CCP5 removes α- and γ-linked glutamates from microtubules, soluble tubulin, and synthetic peptides. Conclusion: CCP5 is not specific for γ-linked glutamate or for a specific form of tubulin. Significance: CCP5 is an important tubulin code-modifying enzyme.

Original language	English (US)
Pages (from-to)	30445-30453
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	42
DOIs	https://doi.org/10.1074/jbc.M113.497917
State	Published - Oct 18 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M113.497917

Cite this

@article{ebf409adcc0d4262b8107ea4d0a2244e,

title = "Cytosolic carboxypeptidase 5 removes α- And γ-linked glutamates from tubulin",

abstract = "Background: Cytosolic carboxypeptidase 5 (CCP5) was proposed to selectively cleave γ-linked glutamate from tubulin side chains, but not α-linked glutamates. Results: Purified CCP5 removes α- and γ-linked glutamates from microtubules, soluble tubulin, and synthetic peptides. Conclusion: CCP5 is not specific for γ-linked glutamate or for a specific form of tubulin. Significance: CCP5 is an important tubulin code-modifying enzyme.",

author = "Iryna Berezniuk and Lyons, {Peter J.} and Sironi, {Juan J.} and Hui Xiao and Mitsutoshi Setou and Angeletti, {Ruth H.} and Koji Ikegami and Fricker, {Lloyd D.}",

year = "2013",

month = oct,

day = "18",

doi = "10.1074/jbc.M113.497917",

language = "English (US)",

volume = "288",

pages = "30445--30453",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "42",

}

TY - JOUR

T1 - Cytosolic carboxypeptidase 5 removes α- And γ-linked glutamates from tubulin

AU - Berezniuk, Iryna

AU - Lyons, Peter J.

AU - Sironi, Juan J.

AU - Xiao, Hui

AU - Setou, Mitsutoshi

AU - Angeletti, Ruth H.

AU - Ikegami, Koji

AU - Fricker, Lloyd D.

PY - 2013/10/18

Y1 - 2013/10/18

N2 - Background: Cytosolic carboxypeptidase 5 (CCP5) was proposed to selectively cleave γ-linked glutamate from tubulin side chains, but not α-linked glutamates. Results: Purified CCP5 removes α- and γ-linked glutamates from microtubules, soluble tubulin, and synthetic peptides. Conclusion: CCP5 is not specific for γ-linked glutamate or for a specific form of tubulin. Significance: CCP5 is an important tubulin code-modifying enzyme.

AB - Background: Cytosolic carboxypeptidase 5 (CCP5) was proposed to selectively cleave γ-linked glutamate from tubulin side chains, but not α-linked glutamates. Results: Purified CCP5 removes α- and γ-linked glutamates from microtubules, soluble tubulin, and synthetic peptides. Conclusion: CCP5 is not specific for γ-linked glutamate or for a specific form of tubulin. Significance: CCP5 is an important tubulin code-modifying enzyme.

UR - http://www.scopus.com/inward/record.url?scp=84886940863&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84886940863&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.497917

DO - 10.1074/jbc.M113.497917

M3 - Article

C2 - 24022482

AN - SCOPUS:84886940863

SN - 0021-9258

VL - 288

SP - 30445

EP - 30453

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 42

ER -

Cytosolic carboxypeptidase 5 removes α- And γ-linked glutamates from tubulin

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this