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First published online April 24, 2006

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Golgi sorting - guilty by association?

Proteins exiting the Golgi can be routed to various destinations, including the cell surface and secretory granules. In cells that exhibit high levels of regulated secretion, an important question is how cells ensure that luminal proteins destined for constitutive secretion do not end up in secretory granules. One possibility is that they lack a sorting signal that directs them to these granules - so-called `sorting for entry'. However, most studies suggest they enter granules by default and are then removed/excluded during granule maturation - `sorting by retention'. Peter Arvan and co-workers have examined these possibilities by following the trafficking of two proteins (SEAP and Cab45₃₆₁) that have had their sorting signals removed so that they are constitutively secreted (see p. 1833). SEAP appears to travel via the secretory granules. The Cab45₃₆₁ mutant, by contrast, is excluded from these. Interestingly, the authors show it remains associated with the membrane if the organelles are permeabilized. Their findings thus provide some of the first evidence for constitutive secretion of a protein without passage through immature granules. Perhaps more intriguingly, they also indicate that the luminal face of Golgi/post-Golgi membranes might have a role in capture of constitutively secreted cargo.

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Related articles in JCS:

Lumenal protein sorting to the constitutive secretory pathway of a regulated secretory cell

Roberto Lara-Lemus, Ming Liu, Mark D. Turner, Philipp Scherer, Gudrun Stenbeck, Puneeth Iyengar, and Peter Arvan
JCS 2006 119: 1833-1842. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?