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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Rodríguez-Crespo I,Yélamos B,Roncal F,Albar JP,Ortiz de Montellano PR,Gavilanes F

doi

10.1016/s0014-5793(01)02718-1

keywords:

subject

Has Abstract

pub_date

2001-08-17 00:00:00

pages

135-41

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014579301027181

journal_volume

503

pub_type

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