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Clathrin light chain b is capable of affecting potently a major protein phosphatase from microtubules (MT‐PP1)
Author(s) -
Hiraga Akira,
Morrice Nick,
Honda Eiko,
Tamura Shinri,
Munakata Hiroshi
Publication year - 2006
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/j.febslet.2005.12.105
Subject(s) - clathrin , phosphatase , protein subunit , chemistry , microtubule , immunoglobulin light chain , protein phosphatase 2 , biochemistry , microbiology and biotechnology , endocytosis , phosphorylation , antibody , biology , receptor , immunology , gene
Clathrin light chain (CL) b purified from bovine brain postmicrotubule supernatant and identified by mass spectrometry potently inhibited a catalytic activity of a major protein phosphatase (PP) that was copurified with microtubules and recognized by antiPP1 antibodies. CLb similarly affected the catalytic subunit and holoenzyme of the PP, little inhibiting the activity of PP2A. Although the CLb from clathrin‐coated vesicles was several hundredfold weaker than our purified CLb, the CLb in the postmicrotubule supernatant, independent of whether it was sedimentable or soluble, was as active as the purified CLb. Thus CLb may be a potent regulator of the PP.