TY - JOUR
T1 - 18 kDa microtubule-associated protein
T2 - identification as a new light chain (LC-3) of microtubule-associated protein 1 (MAP-1)
AU - Kuznetsov, Sergei A.
AU - Gelfand, Vladimir I.
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1987/2/9
Y1 - 1987/2/9
N2 - SDS gel electrophoresis of microtubule proteins obtained from bovine brain by polymerization cycles revealed a new protein of 18 kDa. This protein was copolymerized with tubulin and its stoichiometry to tubulin remained constant for at least 5 cycles of assembly. Moreover, this protein remained bound to microtubules stabilized with 10 μM taxol and pelleted through a 4 M glycerol cushion. The same 18 kDa protein was found in a purified preparation of the high molecular mass microtubule-associated protein 1 (MAP-1). The 18 kDa protein copurified with the MAP-1 heavy chains during column chromatography on phosphocellulose, DEAE-cellulose, hydroxyapatite and Bio-Gel A-15m. Incubation of the MAP-1 preparation with a mouse monoclonal antibody to the light chain 1 (LC-1) of MAP-1 and with a second precipitating antibody (a rabbit antibody to mouse IgG) immunoprecipitated from the solution all the known components of MAP-1 (heavy chains, LC-1, LC-2), as well as the 18 kDa protein. Immunoblotting showed, however, that this antibody does not interact directly with the 18 kDa protein. These results indicate that the 18 kDa protein forms a complex with all other components of MAP-1. This polypeptide, therefore, is a new light chain (LC-3) of M AP-1.
AB - SDS gel electrophoresis of microtubule proteins obtained from bovine brain by polymerization cycles revealed a new protein of 18 kDa. This protein was copolymerized with tubulin and its stoichiometry to tubulin remained constant for at least 5 cycles of assembly. Moreover, this protein remained bound to microtubules stabilized with 10 μM taxol and pelleted through a 4 M glycerol cushion. The same 18 kDa protein was found in a purified preparation of the high molecular mass microtubule-associated protein 1 (MAP-1). The 18 kDa protein copurified with the MAP-1 heavy chains during column chromatography on phosphocellulose, DEAE-cellulose, hydroxyapatite and Bio-Gel A-15m. Incubation of the MAP-1 preparation with a mouse monoclonal antibody to the light chain 1 (LC-1) of MAP-1 and with a second precipitating antibody (a rabbit antibody to mouse IgG) immunoprecipitated from the solution all the known components of MAP-1 (heavy chains, LC-1, LC-2), as well as the 18 kDa protein. Immunoblotting showed, however, that this antibody does not interact directly with the 18 kDa protein. These results indicate that the 18 kDa protein forms a complex with all other components of MAP-1. This polypeptide, therefore, is a new light chain (LC-3) of M AP-1.
KW - Immunoprecipitation
KW - Microtubule
KW - Microtubule-associated protein 1
UR - http://www.scopus.com/inward/record.url?scp=0023156677&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023156677&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(87)81574-0
DO - 10.1016/0014-5793(87)81574-0
M3 - Article
C2 - 3803603
AN - SCOPUS:0023156677
VL - 212
SP - 145
EP - 148
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -