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Evidence against structural and functional identity of microtubule‐associated protein 1B and proteoglycan claustrin
Author(s) -
Tögel Martin,
Wiche Gerhard,
Propst Friedrich
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)00104-5
Subject(s) - proteoglycan , microtubule , extracellular , amino acid , complementary dna , extracellular matrix , epitope , intracellular , microbiology and biotechnology , microtubule associated protein , chemistry , biochemistry , biology , genetics , gene , antibody
Recently, the concept of microtubule‐associated protein 1B as an intracellular 2460 amino acid protein was challenged by the suggestion that only the N‐terminal 1022 codons are utilized and encode the core protein of the extracellular proteoglycan claustrin (Burg and Cole (1994) J. Neurobiol. 25, 1–22). We expressed this N‐terminal MAP1B fragment in tissue culture cells and found that it bound to microtubules and was not localized in the extracellular matrix. In addition, epitope mapping demonstrated that MAP1B consisted of more than 1022 amino acids and that the reported cDNA of claustrin is incomplete.