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Review
. 2007 Apr 23;177(2):191-6.
doi: 10.1083/jcb.200701024. Epub 2007 Apr 16.

Sending proteins to dense core secretory granules: still a lot to sort out

Jimmy D Dikeakos  1 , Timothy L Reudelhuber
Affiliations
Review

Sending proteins to dense core secretory granules: still a lot to sort out

Jimmy D Dikeakos et al. J Cell Biol. .

Abstract

The intracellular sorting of peptide hormone precursors to the dense core secretory granules (DCSGs) is essential for their bioactivation. Despite the fundamental importance of this cellular process, the nature of the sorting signals for entry of proteins into DCSGs remains a source of vigorous debate. This review highlights recent discoveries that are consistent with a model in which several protein domains, acting in a cell-specific fashion and at different steps in the sorting process, act in concert to regulate the entry of proteins into DCSGs.

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Figures

Figure 1.
Figure 1.
Proteins sorted to DCSGs can be functionally subdivided into three groups. Tethers (red) either traverse or associate with membranes. Many DCSG cargo proteins also aggregate to form the dense core (blue), and these aggregates may contain more than one protein. Some DCSG proteins associate with membrane tethers (arrows). The yellow boxes indicate the various protein domains or mechanisms that have been implicated in DCSG sorting. Note that some proteins (such as insulin) may have multiple DCSG sorting mechanisms. See text for details.
See this image and copyright information in PMC

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