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J. Biol. Chem., Vol. 276, Issue 16, 13127-13135, April 20, 2001
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From the The role of
Gaf-1, a
-SNAP-binding Protein Associated with
the Mitochondria*
§,,
Department of Biochemistry, University of
Kentucky College of Medicine, Lexington, Kentucky 40536 and the
¶ Roy M. and Phyllis Gough Huffington Center on Aging, Departments
of Molecular and Cellular Biology and Dermatology, Baylor College of
Medicine, Veterans Affairs Medical Center, Houston, Texas 77030
/
-SNAP (Soluble NSF Attachment
Protein) in vesicular trafficking is well established; however, the
function of the ubiquitously expressed 
-SNAP remains unclear. To
further characterize the cellular role of this enigmatic protein, a
two-hybrid screen was used to identify new, -SNAP-binding proteins
and to uncover potentially novel functions for -SNAP. One such
SNAP-binding protein, termed Gaf-1 (-SNAP associate factor-1)
specifically binds - but not -SNAP. The full-length Gaf-1 (75 kDa) is ubiquitously expressed and is found stoichiometrically
associated with -SNAP in cellular extracts. This binding is distinct
from other SNAP interactions since no -SNAP or NSF coprecipitated
with Gaf-1. Subcellular fractionation and immunofluorescence analysis
show that Gaf-1 is peripherally associated with the outer mitochondrial membrane. Only a fraction of -SNAP was mitochondrial with the balance being either cytosolic or associated with other membrane fractions. GFP--SNAP and the C-terminal domain of Gaf-1 both show a
reticular distribution in HEK-293 cells. This reticular structure
colocalizes with Gaf-1 and mitochondria as well as with microtubules
but not with other cytoskeletal elements. These data identify a class
of -SNAP interactions that is distinct from other members of the
SNAP family and point to a potential role for -SNAP in mitochondrial dynamics.
*
This work was supported by Grant HL56652 from the NHLBI,
National Institutes of Health (to S. W. W.), Grant 0020471B
from the American Heart Association, Ohio Valley Affiliate (to D. C.), and Grant AG-3663 from the NIA, National Institutes of Health (to
E. E. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Biochemistry, University of Kentucky College of Medicine, 800 Rose St., Lexington, KY 40536. Tel.: 859-257-4882; Fax: 859-323-1037; E-mail: whitehe@pop.uky.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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