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Published 9 July 2001. doi:10.1083/jcb.1541ITI6
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© The Rockefeller University Press, 0021-9525/2001/7/11-b $5.00
The Journal of Cell Biology, Volume 154, Number 1, July 9, 2001 11-b-11


In This Issue

Clumping lysosomes


Overexpression of human Vam6p (red) promotes clustering and fusion of lysosomes (green).

Caplan et al. (page 109)find evidence that human Vam6 protein is a mammalian tethering or docking factor with the intrinsic ability to promote lysosome fusion in vivo. The protein is related to a member of a vacuole-fusion complex in budding yeast, but has a unique citron homology domain that is required for lysosome clustering and fusion. Although Rab7 can induce lysosome fusion in yeast, dominant-negative Rab7 does not block hVam6p activity, suggesting that the human protein operates either downstream of, or in parallel to Rab7. {blacksquare}



Alan W. Dove

alanwdove{at}earthlink.net


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Related Article

Human Vam6p promotes lysosome clustering and fusion in vivo
Steve Caplan, Lisa M. Hartnell, Rubén C. Aguilar, Naava Naslavsky, and Juan S. Bonifacino
J. Cell Biol. 2001 154: 109-122. [Abstract] [Full Text] [PDF]




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