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

Dynein is a minus end-directed microtubule motor that serves multiple cellu lar functions. We have performed a fine mapping of the 8 kDa dynein light c hain (LC8) binding sites throughout the development of a library of consecu tive synthetic dodecapeptides covering the amino acid sequences of the vari ous proteins known to interact with this dynein member according to the yea st two hybrid system. Two different consensus sequences were identified: GI QVD present in nNOS, in DNA cytosine methyl transferase and also in GKAP, w here it is present twice in the protein sequence. The other LC8 binding mot if 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 viru ses known to associate with microtubules during retrograde transport from t he plasma membrane to the nucleus during viral infection. (C) 2001 Publishe d by Elsevier Science B.V. on behalf of the Federation of European Biochemi cal Societies.