Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain.

Authors:
Haruki Hasegawa, PhD
Haruki Hasegawa, PhD
Amgen Inc.
Principal Scientist
Protein trafficking Protein biosynthesis
South San Francisco, CA | United States
Sara Zinsser
Sara Zinsser
University of Michigan
United States
Einar Osland Vik-Mo
Einar Osland Vik-Mo
Institute for Surgical Research
Norway
Svend Davanger
Svend Davanger
Institute of Basic Medical Science
Peshawar | Pakistan
Jesse C Hay
Jesse C Hay
The University of Montana
Missoula | United States

Mol Biol Cell 2003 Feb;14(2):698-720

University of Michigan, Department of Molecular, Cellular, and Developmental Biology, Ann Arbor 48109-1048, USA.

SNAREs are required for specific membrane fusion throughout the endomembrane system. Here we report the characterization of rat ykt6, a prenylated SNARE selectively expressed in brain neurons. Immunofluorescence microscopy in neuronal and neuroendocrine cell lines revealed that membrane-associated ykt6 did not colocalize significantly with any conventional markers of endosomes, lysosomes, or the secretory pathway. However, ykt6-containing membranes displayed very minor overlaps with lysosomes and dense-core secretory granules and were similar to lysosomes in buoyant density. Thus, ykt6 appears to be specialized for the trafficking of a unique membrane compartment, perhaps related to lysosomes, involved in aspects of neuronal function. Targeting of this SNARE to the ykt6 compartment was mediated by its profilin-like amino-terminal domain, even in the absence of protein prenylation. Although several other R-SNAREs contain related amino-terminal domains, only the ykt6 version was able to confer the specialized localization. Rat ykt6, which contains an arginine in its SNARE motif zero-layer, was found to behave like other R-SNAREs in its SNARE assembly properties. Interestingly, cytosolic ykt6, constituting more than half of the total cellular pool, appeared to be conformationally inactive for SNARE complex assembly, perhaps indicative of a regulatory mechanism that prevents promiscuous and potentially deleterious SNARE interactions.

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http://dx.doi.org/10.1091/mbc.e02-09-0556DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC150002PMC

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February 2003
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