Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique

FEBS Letters

Gavilanes, Francisco¹  Yélamos, Belén¹  Albar, Juan Pablo²  Rodrı́guez-Crespo, Ignacio¹  Roncal, Fernando²  Ortiz de Montellano, Paul R.³ 

[1] Departamento de Bioquı́mica y Biologı́a Molecular, Facultad de Ciencias Quı́micas, Universidad Complutense de Madrid, 28040 Madrid, Spain;Departamento de Inmunologı́a y Oncologı́a, Centro Nacional de Biotecnologı́a, CSIC, Campus de la Universidad Autónoma de Madrid, 28049 Madrid, Spain;Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, 513 Parnassus Ave, San Francisco, CA 94143-0446, USA

关键词: Migration;    Microtubule;    Dynein;    Nitric oxide;    Yeast two hybrid;    Pepscan;    LC8;    8 kDa dynein light chain;    GKAP;    guanylate kinase domain-associated protein;    HC;    heavy chain;    IC;    intermediate chain;    KRAB;    Krüppel-associated box;    LC;    light chain;    LIC;    light intermediate chain;    nNOS;    neuronal nitric oxide synthase;   

DOI  :  10.1016/S0014-5793(01)02718-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Dynein is a minus end-directed microtubule motor that serves multiple cellular functions. We have performed a fine mapping of the 8 kDa dynein light chain (LC8) binding sites throughout the development of a library of consecutive synthetic dodecapeptides covering the amino acid sequences of the various proteins known to interact with this dynein member according to the yeast two hybrid system. Two different consensus sequences were identified: GIQVD present in nNOS, in DNA cytosine methyl transferase and also in GKAP, where it is present twice in the protein sequence. The other LC8 binding motif is KSTQT, present in Bim, dynein heavy chain, Kid-1, protein 4 and also in swallow. Interestingly, this KSTQT motif is also present in several viruses known to associate with microtubules during retrograde transport from the plasma membrane to the nucleus during viral infection.

【 授权许可】

Unknown