Zuleger, Nikolaj and Kelly, David A. and Richardson, A Christine and Kerr, Alistair R.W. and Goldberg, Martin W. and Goryachev, Andrew B. and Schirmer, Eric C. (2011) 'System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics.', Journal of cell biology., 193 (1). pp. 109-123.
The nuclear envelope contains >100 transmembrane proteins that continuously exchange with the endoplasmic reticulum and move within the nuclear membranes. To better understand the organization and dynamics of this system, we compared the trafficking of 15 integral nuclear envelope proteins using FRAP. A surprising 30-fold range of mobilities was observed. The dynamic behavior of several of these proteins was also analyzed after depletion of ATP and/or Ran, two functions implicated in endoplasmic reticulum–inner nuclear membrane translocation. This revealed that ATP- and Ran-dependent translocation mechanisms are distinct and not used by all inner nuclear membrane proteins. The Ran-dependent mechanism requires the phenylalanine-glycine (FG)-nucleoporin Nup35, which is consistent with use of the nuclear pore complex peripheral channels. Intriguingly, the addition of FGs to membrane proteins reduces FRAP recovery times, and this also depends on Nup35. Modeling of three proteins that were unaffected by either ATP or Ran depletion indicates that the wide range in mobilities could be explained by differences in binding affinities in the inner nuclear membrane.
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|Publisher Web site:||http://dx.doi.org/10.1083/jcb.201009068|
|Publisher statement:||© 2011 Zuleger et al. This article is distributed under the terms of an Attribution– Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).|
|Record Created:||04 May 2011 09:50|
|Last Modified:||04 May 2011 13:10|
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