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J. Cell Biol.,
Volume 141, Number 1, April 6, 1998 143-153
§
* Department of Neuroscience, We have identified a novel generally expressed homologue of the erythrocyte membrane cytoskeletal protein 4.1, named 4.1G, based on the interaction of its COOH-terminal domain (CTD) with the
immunophilin FKBP13. The 129-amino acid peptide,
designated 4.1G-CTD, is the first known physiologic
binding target of FKBP13. FKBP13 is a 13-kD protein
originally identified by its high affinity binding to the
immunosuppressant drugs FK506 and rapamycin (Jin, Y., M.W. Albers, W.S. Lane, B.E. Bierer, and S.J.
Burakoff. 1991. Proc. Natl. Acad. Sci. USA. 88:6677-
6681); it is a membrane-associated protein thought to
function as an ER chaperone (Bush, K.T., B.A. Henrickson, and S.K. Nigam. 1994. Biochem. J. [Tokyo].
303:705-708). We report the specific association of
FKBP13 with 4.1G-CTD based on yeast two-hybrid, in
vitro binding and coimmunoprecipitation experiments.
The histidyl-proline moiety of 4.1G-CTD is required for FKBP13 binding, as indicated by yeast experiments
with truncated and mutated 4.1G-CTD constructs. In
situ hybridization studies reveal cellular colocalizations
for FKBP13 and 4.1G-CTD throughout the body during development, supporting a physiologic role for the
interaction. Interestingly, FKBP13 cofractionates with
the red blood cell homologue of 4.1 (4.1R) in ghosts, inside-out vesicles, and Triton shell preparations. The
identification of FKBP13 in erythrocytes, which lack
ER, suggests that FKBP13 may additionally function as
a component of membrane cytoskeletal scaffolds.
Department of Pharmacology and Molecular Sciences, and § Department of Psychiatry and
Behavioral Sciences, The Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205; and Life Sciences
Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720
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