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 Lettjournal_title
FEBS lettersauthors
Rodríguez-Crespo I,Yélamos B,Roncal F,Albar JP,Ortiz de Montellano PR,Gavilanes Fdoi
10.1016/s0014-5793(01)02718-1keywords:
subject
Has Abstractpub_date
2001-08-17 00:00:00pages
135-41issue
2-3eissn
0014-5793issn
1873-3468pii
S0014579301027181journal_volume
503pub_type
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