Premium
Neuraxin corresponds to a C‐terminal fragment of microtubule‐associated protein 5 (MAP5)
Author(s) -
Kirsch Joachim,
Littauer Uriel Z.,
Schmitt Bertram,
Prior Peter,
Thomas Leo,
Betz Heinrich
Publication year - 1990
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 - 10.1016/0014-5793(90)80205-w
Subject(s) - tubulin , microtubule , fragment (logic) , biology , homology (biology) , microbiology and biotechnology , binding protein , microtubule associated protein , binding site , biochemistry , amino acid , gene , computer science , programming language
From cloned DNA, neuraxin has been identified as a tubulin binding protein of predicted molecular weight of 94 kDa. The deduced sequence of the rat protein exhibits high homology to the C‐terminal region of mouse microtubule‐associated protein 5 (MAP5). Here, we show that different neuraxin antibodies recognize MAP5, but fail to detect a protein of 94 kDa, in subcellular and microtubular fractions of the rat central nervous system. Furthermore, tubulin binding by neuraxin was found to be dependent on taxol. These data are consistent with neuraxin corresponding to a C‐terminal fragment of MAP5 that contains a low‐affinity tubulin binding site.