Starr Daniel A, Fischer Janice A
Section of Molecular and Cellular Biology, Center for Genetics and Development, University of California, Davis, CA, USA.
Bioessays. 2005 Nov;27(11):1136-46. doi: 10.1002/bies.20312.
A diverse family of proteins has been discovered with a small C-terminal KASH domain in common. KASH domain proteins are localized uniquely to the outer nuclear envelope, enabling their cytoplasmic extensions to tether the nucleus to actin filaments or microtubules. KASH domains are targeted to the outer nuclear envelope by SUN domains of inner nuclear envelope proteins. Several KASH protein genes were discovered as mutant alleles in model organisms with defects in developmentally regulated nuclear positioning. Recently, KASH-less isoforms have been found that connect the cytoskeleton to organelles other than the nucleus. A widened view of these proteins is now emerging, where KASH proteins and their KASH-less counterparts are cargo-specific adaptors that not only link organelles to the cytoskeleton but also regulate developmentally specific organelle movements.
人们发现了一个多样的蛋白质家族,它们具有共同的小C端KASH结构域。KASH结构域蛋白独特地定位于核外膜,使其细胞质延伸部分能够将细胞核与肌动蛋白丝或微管相连。KASH结构域通过内核膜蛋白的SUN结构域靶向核外膜。在发育调控的核定位存在缺陷的模式生物中,几个KASH蛋白基因被发现为突变等位基因。最近,人们发现了无KASH异构体,它们将细胞骨架与细胞核以外的细胞器相连。现在,对这些蛋白质的认识正在拓宽,其中KASH蛋白及其无KASH对应物是货物特异性衔接子,它们不仅将细胞器与细胞骨架相连,还调节发育特异性细胞器运动。