Premium
Mitsugumin23, a novel transmembrane protein on endoplasmic reticulum and nuclear membranes
Author(s) -
Nishi Miyuki,
Komazaki Shinji,
Iino Masamitsu,
Kangawa Kenji,
Takeshima Hiroshi
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00864-3
Subject(s) - endoplasmic reticulum , transmembrane protein , transmembrane domain , microbiology and biotechnology , stim1 , biology , skeletal muscle , cytoplasm , biochemistry , complementary dna , myosin , chemistry , membrane , gene , anatomy , receptor
We report the identification using monoclonal antibody and the primary structure by cDNA cloning of mitsugumin23, a novel transmembrane protein with a molecular mass of ∼23 kDa from skeletal muscle sarcoplasmic reticulum. Mitsugumin23 possesses three putative transmembrane segments, and its carboxy‐terminal hydrophilic region exhibits sequence similarity with the tail‐end portion of the myosin heavy chain. Immunochemical analysis showed that this protein is distributed throughout the outer nuclear membrane and the sarcoplasmic reticulum including the terminal cisternae at the triad junction in skeletal muscle cells. Furthermore, RNA blotting and immunohistochemical experiments demonstrated that mitsugumin23 is distributed among a wide variety of cell types in various tissues. The distribution and primary structure indicate the possibility that mitsugumin23 interacts with cytoplasmic protein(s) and participates in a housekeeping function on the intracellular organelle membranes.