Document Detail

SUMO modification modulates the activity of calpain-2.
MedLine Citation:
PMID:  19422794     Owner:  NLM     Status:  MEDLINE    
Small ubiquitin-like modifier (SUMO) modification has been shown to be involved in the regulation of various cellular processes including gene transcription, nucleocytoplasmic transport, cell cycle, DNA repair, stress response, and signal transduction. However, very little is known about the process of cell migration being modulated by SUMO modification. Here, we show that calpain-2, a protease involved in cell motility, can be SUMO modified at lysine residue 390. Converting the SUMO acceptor lysine residue to arginine residue significantly attenuated calpain-2 activity, correlating well with a loss of calpain-2-elicited cell motility. Accordingly, expression of SENP1 could abrogate calpain-2 sumoylation, causing an inhibition on calpain-2-dependent activity and cell motility. These results not only identify calpain-2 as a substrate for sumoylation but also provide an important role of sumoylation in regulating cell migration.
Hsueh-Chun Wang; Yen-Sung Huang; Chun-Chen Ho; Jen-Chong Jeng; Hsiu-Ming Shih
Related Documents :
10712904 - Contact dynamics during keratocyte motility.
17438554 - Cilia containing 9 + 2 structures grown from immortalized cells.
16819464 - Transcriptional regulation of dictyostelium pattern formation.
25313354 - Inhibition of nek2 by small molecules affects proteasome activity.
3264534 - B cell precursors in chick embryos surgically bursectomized at 72 h of incubation.
22179484 - Cell growth of bg-1 ovarian cancer cells is promoted by di-n-butyl phthalate and hexabr...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-05-05
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  384     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2009 Jul 
Date Detail:
Created Date:  2009-05-27     Completed Date:  2009-06-19     Revised Date:  2012-07-11    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  444-9     Citation Subset:  IM    
Graduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan, ROC.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
COS Cells
Calpain / genetics,  metabolism*
Cell Movement*
Cercopithecus aethiops
Endopeptidases / metabolism
Lysine / genetics,  metabolism
SUMO-1 Protein / metabolism*
Reg. No./Substance:
0/SUMO-1 Protein; 56-87-1/Lysine; EC 3.4.-/Endopeptidases; EC 3.4.-/SENP1 protein, human; EC 3.4.22.-/Calpain; EC 2, human

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Single-fluorophore monitoring of DNA hybridization for investigating the effect of secondary structu...
Next Document:  A novel calpastatin-based inhibitor improves postischemic neurological recovery.