We examined the association of a 34-kD light chain component to the heavy chains of MAP-1 using a monoclonal antibody that specifically binds the 34-kD component and labels neuronal microtubules in a specific and saturable manner. Immunoprecipitation of MAP-1 heavy chains together with the 34-kD component by the antibody indicates that the 34-kD polypeptide forms a complex with MAP-1 heavy chains. Both major isoforms of MAP-1 heavy chains (MAP-1A and MAP-1B) were found in the immunoprecipitate. Digestion of MAP-1 with alpha-chymotrypsin and analysis of the chymotryptic peptides reveals a 120-kD fragment of the MAP-1 heavy chain that binds to microtubules and is precipitable with the 34-kD light chain antibody, suggesting that the 34-kD light chain also binds to this domain of the molecule. Since microtubules that contain the 120-kD fragment lack the long lateral projections characteristic of microtubules with intact MAP-1, the 34-kD light chains may be localized at or near the microtubule surface.
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1 March 1986
Article|
March 01 1986
Identification of a 34-kD polypeptide as a light chain of microtubule-associated protein-1 (MAP-1) and its association with a MAP-1 peptide that binds to microtubules.
S A Kuznetsov
V I Rodionov
E S Nadezhdina
D B Murphy
V I Gelfand
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1986) 102 (3): 1060–1066.
Citation
S A Kuznetsov, V I Rodionov, E S Nadezhdina, D B Murphy, V I Gelfand; Identification of a 34-kD polypeptide as a light chain of microtubule-associated protein-1 (MAP-1) and its association with a MAP-1 peptide that binds to microtubules.. J Cell Biol 1 March 1986; 102 (3): 1060–1066. doi: https://doi.org/10.1083/jcb.102.3.1060
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