Cell Biology

Recruitment System

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Science  30 Apr 2004:
Vol. 304, Issue 5671, pp. 651
DOI: 10.1126/science.304.5671.651d

The targeting of peripheral membrane proteins to the Golgi complex is important in order to maintain the distinct identity of membranes as transport vesicles bud off from and fuse with intracellular organelles. Behnia et al. and Setty et al. describe aspects of the targeting mechanism for a family of Golgi proteins, the golgins, that help direct membrane traffic. In yeast cells, the small GTP-binding protein Arl3 (whose human homolog is ARFRP1) is recruited to the Golgi and is responsible for recruiting a second protein, Arl1, that binds to the GRIP domain in golgins and attaches these vesicle-tethering proteins to the Golgi complex. Unlike other Arf-like GTP-binding proteins, Arl3 is not myristoylated, but instead is acetylated at its N-terminal end. The targeting of Arl3 requires the integral membrane protein Sys1, which appears to interact directly with the acetylated tail of Arl3. Thus, Golgi-localized Sys1 recruits acetylated Arl3, which in turn recruits Arl1, which can then recruit golgins. — SMH

Nature Cell Biol. 10.1038/ncb1120; 10.1038/ncb1121 (2004).

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