The 33-residue LIS1 homology (LisH) motif (IPR006594) is found in eukaryotic intracellularproteins involved in microtubule dynamics, cell migration, nucleokinesis andchromosome segregation. The LisH motif is likely to possess a conservedprotein-binding function and it has been proposed that LisH motifs contributeto the regulation of microtubule dynamics, either by mediating dimerization,or else by binding cytoplasmic dynein heavy chain or microtubules directly.The LisH motif is found associated to other domains, such as WD-40 (seePDOC00574), SPRY, Kelch, AAA ATPase, RasGEF, or HEAT (see PDOC50077)[1, 2, 3].The secondary structure of the LisH domain is predicted to be two alpha-helices [4].

The C-terminal to LisH (CTLH) motif is a predicted alpha-helical sequence ofunknown function that is found adjacent to the LisH motif in a number of theseproteins but is absent in other (e.g. LIS1) [4, 4, 4]. The CTLH domain can alsobe found in the absence of the LisH motif, like in:

1. A new sequence motif linking lissencephaly, Treacher Collins and oral-facial-digital type 1 syndromes, microtubule dynamics and cell migration. Hum. Mol. Genet. 10, 2813-20
2. Characterization of a Drosophila melanogaster orthologue of muskelin. Gene 297, 69-78
3. A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM. Gene 303, 47-54

The 33-residue LIS1 homology (LisH) motif (IPR006594Show more...

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