JCB logo
Avanti Polar Lipids
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online 30 December 2002. doi:10.1083/jcb1601iti4
This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by LeBrasseur, N.
Right arrow Search for Related Content
PubMed
Right arrow Articles by LeBrasseur, N.
Related Collections
Right arrowRelated Article
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  
What's this?
© The Rockefeller University Press, 0021-9525/2003/1/7-b $5.00
The Journal of Cell Biology, Volume 160, Number 1, 7-b-7


In This Issue

RNA travels with ZBP1


Lamella-localized ZBP1 (white) granules do not form if ZBP1 cannot bind actin mRNA (right).

On page 77, Farina et al. get a handle on RNA localization machinery by proving that an RNA-binding protein is essential for both mRNA transport and cell motility.

The cell motility connection comes about because localization of the ß-actin mRNA to the lamellae is required for cell polarity and motility in fibroblasts. The new results show that this localization depends on ZBP1, a protein associated with cytoplasmic granules that contain the actin mRNA. ZBP1 bound to the mRNA through two COOH-terminal KH domains that were required for granule formation and attachment to the actin cytoskeleton. NH2-terminal regions of ZBP1 were necessary for granule localization in the lamellae.

Dominant–negative ZBP1 constructs that mislocalized actin RNA inhibited fibroblast motility. Since mRNAs for some actin-associated proteins, such as ARP3, also contain ZBP1-binding sequences, the authors believe that ZBP1 may link several messages involved in motility to a transport complex. But ZBP1 may be more than just a scaffold: a ZBP1 homologue has been linked to translational repression of the insulin-related growth factor. Perhaps ZBP1 also ensures that the actin mRNA is not translated until it reaches its ultimate destination.The group plans to purify ZBP1- associated proteins in the complex to identify the motor responsible for actin-based transport. ZBP1 is also known to be associated with microtubules in neurons, so it may connect to different motors depending on the cell type. {blacksquare}



Nicole LeBrasseur

lebrasn{at}rockefeller.edu


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    What's this?

Related Article

Two ZBP1 KH domains facilitate ß-actin mRNA localization, granule formation, and cytoskeletal attachment
Kim L. Farina, Stefan Hüttelmaier, Kiran Musunuru, Robert Darnell, and Robert H. Singer
J. Cell Biol. 2003 160: 77-87. [Abstract] [Full Text] [PDF]




This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by LeBrasseur, N.
Right arrow Search for Related Content
PubMed
Right arrow Articles by LeBrasseur, N.
Related Collections
Right arrowRelated Article
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  
What's this?


  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents