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

Published online 3 April 2006. doi:10.1083/jcb.1731rr3
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 1, 5-5
This Article
Right arrow Full Text (PDF, 1001K)
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.
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?

Research Roundup

Kinesin switch in neurites



Figure 1
Kinesin-1 (red) accumulates specifically in the axon (arrowhead) even before microtubule polarity differs between axon and dendrites.

BANKER/ELSEVIER

Before axon specification, seemingly identical neurites are not so alike after all. New research from Catherine Jacobson, Bruce Schnapp, and Gary Banker (Oregon Heath & Science Center, Portland, OR) reveals a hitherto unseen biochemical distinction in neurites of developing neurons.

The distinction was noted while visualizing a constitutive version of the Kinesin-1 motor, which in mature neurons is found only in the axon. Because the plus ends of axonal microtubules point away from the cell body, whereas those in dendrites face both directions, Kinesin-1's plus end–directed activity could explain this specific accumulation. But the new results show that Kinesin-1 is found in a subset of young neurites, often in just one, at a time when the microtubules in all neurites are still similarly oriented.

The accumulation of Kinesin-1 in a given young neurite was transient—it periodically switched homes until the time at which the axon was specified. With each switch, only one or two neurites contained the motor at a time. To explain the preference of Kinesin-1 for a given neurite, Banker suggests, "the population of microtubules [in that neurite] is distinct. But I'm pretty mystified as to what that difference is."

One of his theories suggests that tubulin is transiently modified posttranslationally in certain neurites. Because Kinesin-1 has a relatively low affinity for microtubules but travels far with each binding, localized modifications that increase its affinity even slightly might strongly favor its accumulation in that neurite.

Stable accumulation of truncated Kinesin-I within a neurite coincided with that neurite's specification as the axon and is now the earliest marker of this event. But, says Banker, "every time you see one of these molecular distinctions, it takes the question one step higher, to ‘what led to that?’" This new question will now haunt neurobiologists, at least for the near future. Formula

Reference:

Jacobson, C., et al. 2006. Neuron. 49:797–804.[CrossRef][Medline]



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



This Article
Right arrow Full Text (PDF, 1001K)
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.
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