spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mollat, P.
Right arrow Articles by Thang, M. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mollat, P.
Right arrow Articles by Thang, M. N.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Journal of Cell Science, Vol 107, Issue 3 427-435, Copyright © 1994 by Company of Biologists

JOURNAL ARTICLES

Species specificity and organ, cellular and subcellular localization of the 100 kDa Ras GTPase activating protein

P Mollat, A Fournier, CZ Yang, E Alsat, Y Zhang, D Evain-Brion, J Grassi and MN Thang
Unite 245 INSERM, Hopital Saint-Antoine, Paris, France.

A p100-GAP isoform, generated by an alternative splicing mechanism that eliminates the 180 hydrophobic amino acids at the amino terminus of p120-GAP, has been described in human placenta, in addition to the known p120GAP and neurofibromin. This p100-GAP possesses full Ras-GTPase stimulating activity. p120-GAP is ubiquitously localized in the cytosol while the localization of p100-GAP is unknown. Here we have explored the precise localization of p100-GAP and show that p100-GAP is present only in extracts of primate placenta. It is abundant in both human and Maccaca Rhesus placentae, where it is present in far larger amounts than p120-GAP. The p100-GAP is species-specific since it was not detected in the placenta of pig, sheep, mouse or rat. p100-GAP was also found to be organ-specific, since it was not detectable in organs other than the placenta. In this connection, we substantiated our previous finding that p100-GAP is mainly localized in the trophoblasts. Both subcellular trophoblast fractionation and immunofluorescence analyses showed that this protein was distributed between the cytosol, plasma membrane and a fraction bound to the nucleus, but not inside it. This highly restrictive specificity of p100-GAP localization in relation to species, organ and cell type, confirms the extreme singularity of this protein, and strongly suggests a particular specific function in the trophoblast.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 Hum Mol GenetHome page
R. N. Nurtdinov, I. I. Artamonova, A. A. Mironov, and M. S. Gelfand
Low conservation of alternative splicing patterns in the human and mouse genomes
Hum. Mol. Genet., June 1, 2003; 12(11): 1313 - 1320.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. Laverdiere, J. Beaudoin, and A. Lavigueur
Species-specific regulation of alternative splicing in the C-terminal region of the p53 tumor suppressor gene
Nucleic Acids Res., March 15, 2000; 28(6): 1489 - 1497.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1994