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Pubmed Central  Novel functional features of the Lis-H domain:
role in protein dimerization, half-life and cellular
localization.  Gerlitz G, Darhin E, Giorgio G, Franco B, Reiner
O Cell cycle (Georgetown, Tex.)   The presence of a conserved
protein motif usually implies common functional features. Here,
we focused on the LisH (LIS1 homology) domain, which is found in
multiple proteins, and have focused on three involved in human
genetic diseases; LIS1, Transducin beta-like 1X (TBL1) and Oral-
facial-digital type 1 (OFD1). The recently solved structure of
the LisH domain in the N-terminal region of LIS1 depicted it as
a novel dimerization motif. Our findings indicated that the LisH
domain of both LIS1 and TBL1 is essential for in vitro
oligomerization. Furthermore, our study disclosed novel in vivo
features of the LisH motif. Mutations in conserved LisH amino
acids significantly reduced both the protein half-life of LIS1,
TBL1, and OFD1, and drama