Background |
There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. This protein is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. This protein also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms. |
Manufacturers Research Area |
Signal Transduction, Kinase, Serine/threonine kinases, Tyrosine kinases, Cell Biology & Developmental Biology, Cytoskeleton, Microfilaments, Microtubules, Actins, TGF-b-Smad Signaling Pathway, Immunology & Inflammation, Neuroscience, Cell Type Marker, Neuron marker, Growth Cone, |