大约有40个已知的真核LIM蛋白，因此命名为它们包含的LIM结构域。LIM结构域是高度保守的富含半胱氨酸的结构，含有2个锌指尽管锌指通常通过与dna或rna结合而起作用，lim基序可能介导蛋白质-蛋白质相互作用。lim激酶-1和lim激酶-2属于一个小的亚家族，具有2个n端lim基序和一个c端蛋白激酶结构域的独特组合。limk1是一种丝氨酸/苏氨酸激酶，通过肌动蛋白结合因子cofilin的磷酸化和失活来调节肌动蛋白聚合。这种蛋白在发育过程中广泛表达，并在许多与细胞骨架结构相关的细胞过程中发挥作用这种蛋白质也刺激轴突生长，可能在大脑发育中发挥作用limk1半合子性与williams综合征视空间结构认知受损有关。选择性剪接导致编码不同亚型的多个转录变体。[由RefSeq提供，2011年2月]
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.[provided by RefSeq, Feb 2011]