Document Detail


Epidermal growth factor-induced mobilization of a ganglioside-specific sialidase (NEU3) to membrane ruffles.
MedLine Citation:
PMID:  16765317     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human ganglioside-specific sialidase, NEU3, localized at cell membranes is thought to regulate various biological processes at cell surfaces. We here explored functional subcellular localization of the sialidase by immunofluorescence and found accumulation at leading edges of cell membranes in the presence of serum in culture. In response to EGF, the sialidase redistributed rapidly to ruffling cell membranes of squamous carcinoma A431 cells and co-localized with Rac-1. NEU3 overexpression enhanced Rac-1 activation and cell migration as compared with controls in HeLa cells as well as in A431 cells. Consistent with co-localization with Rac-1 by immunofluorescence, NEU3 was found to co-precipitate with activated Rac bound to GST-PAK-1 fusion protein. NEU3 silencing by siRNA, in contrast, resulted in inhibition of Rac-1 activation. These results indicate that NEU3 is able to mobilize to membrane ruffles in response to growth stimuli and activate the Rac-1 signaling by co-localization with Rac-1, leading to increased cell motility.
Authors:
Kazunori Yamaguchi; Keiko Hata; Tadashi Wada; Setsuko Moriya; Taeko Miyagi
Related Documents :
20043047 - Shrna targeting hdgf suppressed cell growth and invasion of squamous cell lung cancer.
17900607 - Topography of signaling molecules as detected by electron microscopy on plasma membrane...
20224097 - Pseudoangiomatous squamous cell carcinoma in the oral cavity of a dog.
17912427 - Overexpression of septin1: possible contribution to the development of oral cancer.
9486797 - Analysis of the early embryonic cell cycles of xenopus; regulation of cell cycle length...
15486067 - Activation of the pi3k/mtor pathway by bcr-abl contributes to increased production of r...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-06-05
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  346     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2006 Jul 
Date Detail:
Created Date:  2006-06-20     Completed Date:  2006-08-30     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  484-90     Citation Subset:  IM    
Affiliation:
Division of Biochemistry, Miyagi Cancer Center Research Institute, Natori, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Cell Membrane Structures / metabolism*
Cell Movement
Cercopithecus aethiops
Enzyme Activation
Epidermal Growth Factor / physiology*
Humans
Mice
Neuraminidase / biosynthesis,  genetics,  metabolism*
Protein Binding
Protein Transport
Protein-Serine-Threonine Kinases / metabolism
p21-Activated Kinases
rac1 GTP-Binding Protein / metabolism
Chemical
Reg. No./Substance:
0/Pak1 protein, mouse; 62229-50-9/Epidermal Growth Factor; EC 2.7.11.1/PAK1 protein, human; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/p21-Activated Kinases; EC 3.2.1.18/Neu3 protein, human; EC 3.2.1.18/Neuraminidase; EC 3.6.5.2/rac1 GTP-Binding Protein

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


Previous Document:  Heterologous expression and localization of gentisate transporter Ncg12922 from Corynebacterium glut...
Next Document:  Intrinsic radiation resistance in human chondrosarcoma cells.