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J Biol Chem, Vol. 274, Issue 41, 29282-29288, October 8, 1999
From the Here we describe the isolation and partial
characterization of a new muscle-specific protein (Melusin) which
interacts with the integrin cytoplasmic domain. The cDNA encoding
Melusin was isolated in a two-hybrid screening of a rat neonatal heart
library using
Melusin Is a New Muscle-specific Interactor for
1
Integrin Cytoplasmic Domain
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,,, and
Department of Genetics, Biology and
Biochemistry, University of Torino, Torino 10126, Italy, the
¶ Immunogenetic and Experimental Oncology Center, CNR, Torino
10126, Italy, and the Institute of Genetics, University of Bari,
Bari 70122, Italy
1A and 1D integrin
cytoplasmic regions as baits. Melusin is a cysteine-rich cytoplasmic
protein of 38 kDa, with a stretch of acidic amino acid residues at the
extreme carboxyl-terminal end. In addition, putative binding sites for
SH3 and SH2 domains are present in the amino-terminal half of the
molecule. Chromosomic analysis showed that melusin gene
maps at Xq12.1/13 in man and in the synthenic region X band D in mouse.
Melusin is expressed in skeletal and cardiac muscles but not in smooth
muscles or other tissues. Immunofluorescence analysis showed that
Melusin is present in a costamere-like pattern consisting of two rows
flanking 
-actinin at Z line. Its expression is up-regulated during
in vitro differentiation of the C2C12 murine myogenic cell
line, and it is regulated during in vivo skeletal muscle
development. A fragment corresponding to the tail region of Melusin
interacted strongly and specifically with 1 integrin
cytoplasmic domain in a two-hybrid test, but the full-length protein
did not. Because the tail region of Melusin contains an acidic amino
acid stretch resembling high capacity and low affinity calcium binding
domains, we tested the possibility that Ca2+ regulates
Melusin-integrin association. In vitro binding experiments demonstrated that interaction of full-length Melusin with
detergent-solubilized integrin heterodimers occurred only in absence of
cations, suggesting that it can be regulated by intracellular signals
affecting Ca2+ concentration.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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