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Identification of Acan125 as a myosin-I-binding protein present with myosin-I on cellular organelles of Acanthamoeba.

作者信息

Xu P, Zot A S, Zot H G

机构信息

Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235-9040, USA.

出版信息

J Biol Chem. 1995 Oct 27;270(43):25316-9. doi: 10.1074/jbc.270.43.25316.

Abstract

We have discovered the first protein to bind to a non-filamentous myosin, aside from actin. This protein, Acan125, is a 125-kDa protein from Acanthamoeba that associates with the SH3 domain of Acanthamoeba myosin-IC and not the SH3 domain of human fodrin. Antibodies raised against Acan125 recognize a single protein of 125 kDa from a whole cell lysate of Acanthamoeba; antibodies to myosin-I (M1.7 and M1.8) do not recognize Acan125 on the same blot. Double labeling of Acanthamoeba show Acan125 and myosin-I to be present on the same intracellular organelle, most likely amoebastomes. Immunoprecipitation with either anti-myosin-I or anti-Acan125 antibodies coprecipitates both Acan125 and myosin-I from a lysate of Acanthamoeba, demonstrating that Acan125 interacts with native myosin-I.

摘要

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