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J. Biol. Chem., Vol. 276, Issue 16, 13127-13135, April 20, 2001
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-SNAP-binding Protein Associated with
the Mitochondria*
§,
,
From the The role of
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.
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.
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