PMID- 10506186
OWN - NLM
STAT- MEDLINE
DCOM- 19991109
LR  - 20220129
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 41
DP  - 1999 Oct 8
TI  - Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic
      domain.
PG  - 29282-8
AB  - 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 beta(1)A and beta(1)D 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 alpha-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 beta(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 Ca(2+) 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 Ca(2+) concentration.
FAU - Brancaccio, M
AU  - Brancaccio M
AD  - Department of Genetics, University of Torino, Torino 10126, Italy.
FAU - Guazzone, S
AU  - Guazzone S
FAU - Menini, N
AU  - Menini N
FAU - Sibona, E
AU  - Sibona E
FAU - Hirsch, E
AU  - Hirsch E
FAU - De Andrea, M
AU  - De Andrea M
FAU - Rocchi, M
AU  - Rocchi M
FAU - Altruda, F
AU  - Altruda F
FAU - Tarone, G
AU  - Tarone G
FAU - Silengo, L
AU  - Silengo L
LA  - eng
SI  - GENBANK/AF140690
SI  - GENBANK/AF140691
GR  - E.0672/TI_/Telethon/Italy
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (ITGB1BP2 protein, human)
RN  - 0 (Integrin beta1)
RN  - 0 (Itgb1bp2 protein, mouse)
RN  - 0 (Muscle Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Fusion Proteins)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Animals, Newborn
MH  - Calcium/metabolism
MH  - Carrier Proteins/chemistry/*genetics/metabolism
MH  - Cell Line
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - Cytoplasm/chemistry
MH  - *Cytoskeletal Proteins
MH  - Fluorescent Antibody Technique
MH  - Gene Expression Regulation, Developmental
MH  - In Situ Hybridization, Fluorescence
MH  - Integrin beta1/chemistry/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Muscle Proteins/chemistry/*genetics/metabolism
MH  - Muscle, Skeletal/embryology/metabolism
MH  - Myocardium/metabolism
MH  - RNA, Messenger/metabolism
MH  - Rats
MH  - Recombinant Fusion Proteins/metabolism
MH  - Regeneration
MH  - Sequence Homology, Amino Acid
MH  - X Chromosome
MH  - src Homology Domains
EDAT- 1999/10/03 00:00
MHDA- 1999/10/03 00:01
CRDT- 1999/10/03 00:00
PHST- 1999/10/03 00:00 [pubmed]
PHST- 1999/10/03 00:01 [medline]
PHST- 1999/10/03 00:00 [entrez]
AID - 10.1074/jbc.274.41.29282 [doi]
AID - S0021-9258(19)51972-X [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 8;274(41):29282-8. doi: 10.1074/jbc.274.41.29282.