JCB logo
amgmicro.com
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online
doi:10.1083/jcb.1781iti3
The Journal of Cell Biology, Vol. 178, No. 1, 3-
The Rockefeller University Press, 0021-9525 $30.00
© Leslie
This Article
Right arrow Full Text (PDF, 896K)
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 Leslie, M.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Leslie, M.
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 Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

In This Issue

Mitochondria on the MARCH



Figure 1
Mitochondria (red) are stickier in cells that make faulty MARCH5 (green).

Breaking up isn't hard to do for mitochondria, which are continually separating and merging. On page 71, Karbowski et al. pinpoint a protein that prods the organelles to go their own way.

Cells carefully control mitochondrial fusion and fission, and an imbalance between the processes can be disastrous. For example, a faulty fusion-promoting protein triggers dominant optic atrophy, the leading cause of inherited blindness. Researchers know more about the regulation of fusion and fission in yeast than in mammals. But they do know that one of the mammalian proteins essential for mitochondrial breakup is Drp1.

Karbowski et al. pinpointed another, called MARCH5, which colocalizes with Drp1. Although two studies published last year suggested that MARCH5 promoted mitochondrial fusion, the scientists now find the opposite. When they altered cells to produce a defective version of the protein, mitochondria stuck together to form extra-long networks instead of breaking apart. The researchers also observed this abnormal elongation when they added RNAi against MARCH5.

The protein normally spreads out around the mitochondrial membrane, but the mutant MARCH5 clumped. These clusters trapped Drp1. These findings suggest that MARCH5 spurs mitochondrial splitting by helping to direct Drp1 to the future separation site. MARCH5 is a ubiquitin ligase that works by attaching a ubiquitin molecule to its target. The researchers' next move is to track down that target. Formula



Mitch Leslie

mitchleslie{at}comcast.net


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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?

Related Article

The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
Mariusz Karbowski, Albert Neutzner, and Richard J. Youle
J. Cell Biol. 2007 178: 71-84. [Abstract] [Full Text] [PDF]




This Article
Right arrow Full Text (PDF, 896K)
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 Leslie, M.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Leslie, M.
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 Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?


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