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


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online November 24, 2004

Journal of Cell Science 117, 2502e (2004)
© The Company of Biologists Limited
This Article
Right arrow Full Text (PDF)
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 Related articles in JCS
Right arrow Similar articles in this journal
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 Google Scholar
Google Scholar
Right arrow Search for Related Content

In this issue

Insulin PIKs a target


Translocation of vesicles containing the glucose transporter GLUT4 to the surface of fat and muscle cells is an important part of the body's response to insulin. The signalling pathway involved hinges on phosphoinositide 3-kinase (PI3K) and its downstream kinase PKB (also known as Akt); however, the key PKB targets have remained elusive. Jeremy Tavaré and coworkers now unveil one of these: PIKfyve, an enzyme that generates the phospholipid PtdIns(3,5)P2 from PtdIns(3)P (see p. 5985). Identifying PIKfyve as a protein that is phosphorylated in cells stimulated by insulin, the authors show that it is phosphorylated on Ser318 by PKB in vitro and that this increases its activity. They then demonstrate that the PI3K inhibitor wortmannin can block insulin-induced phosphorylation of Ser318 in vivo. Finally, they show that PIKfyve colocalizes with a marker for GLUT4-containing vesicles and can modulate insulin-dependent trafficking of vesicles containing this marker. Their findings thus indicate that PIKfyve is a PKB effector in insulin signalling. However, since it has previously been implicated in endosomal sorting and PKB responds to numerous extracellular stimuli, PIKfyve could have a wider role in signal-regulated membrane trafficking.


Related articles in JCS:

Protein kinase B phosphorylation of PIKfyve regulates the trafficking of GLUT4 vesicles
Daniel C. Berwick, Ghislaine C. Dell, Gavin I. Welsh, Kate J. Heesom, Ingeborg Hers, Laura M. Fletcher, Frank T. Cooke, and Jeremy M. Tavaré
JCS 2004 117: 5985-5993. [Abstract] [Full Text]  




This Article
Right arrow Full Text (PDF)
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 Related articles in JCS
Right arrow Similar articles in this journal
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 Google Scholar
Google Scholar
Right arrow Search for Related Content