|PROSITE documentation PDOC50896 [for PROSITE entry PS50896]|
The 33-residue LIS1 homology (LisH) motif is found in eukaryotic intracellular proteins involved in microtubule dynamics, cell migration, nucleokinesis and chromosome segregation. The LisH motif is likely to possess a conserved protein-binding function and it has been proposed that LisH motifs contribute to 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 (see <PDOC00574>), SPRY, Kelch, AAA ATPase, RasGEF, or HEAT (see <PDOC50077>) [1,2,3].
The secondary structure of the LisH domain is predicted to be two α-helices .
Some proteins known to contain a LisH motif are listed below:
The C-terminal to LisH (CTLH) motif is a predicted α-helical sequence of unknown function that is found adjacent to the LisH motif in a number of these proteins but is absent in other (e.g. LIS1) [1,2,3]. The CTLH domain can also be found in the absence of the LisH motif, like in:
The profiles we developed cover respectively the entire LisH and CTLH motifs.Last update:
February 2003 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Emes R.D. Ponting C.P.|
|Title||A new sequence motif linking lissencephaly, Treacher Collins and oral-facial-digital type 1 syndromes, microtubule dynamics and cell migration.|
|Source||Hum. Mol. Genet. 10:2813-2820(2001).|
|Title||Characterization of a Drosophila melanogaster orthologue of muskelin.|
|3||Authors||Umeda M. Nishitani H. Nishimoto T.|
|Title||A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM.|