KASH 'n Karry: The KASH domain family of cargo‐specific cytoskeletal adaptor proteins
- 19 October 2005
- Vol. 27 (11) , 1136-1146
- https://doi.org/10.1002/bies.20312
Abstract
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. BioEssays 27:1136–1146, 2005.Keywords
This publication has 68 references indexed in Scilit:
- Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeletonExperimental Cell Research, 2004
- The tale of tail-anchored proteinsThe Journal of cell biology, 2003
- ANChors away: an actin based mechanism of nuclear positioningJournal of Cell Science, 2003
- Role of ANC-1 in Tethering Nuclei to the Actin CytoskeletonScience, 2002
- Functional plasticity of CH domainsFEBS Letters, 2001
- Syne-1, A Dystrophin- and Klarsicht-related Protein Associated with Synaptic Nuclei at the Neuromuscular JunctionJournal of Biological Chemistry, 2000
- Nuclear MigrationThe Journal of cell biology, 2000
- Molecular analysis of the klarsicht gene and its role in nuclear migration within differentiating cells of the Drosophila eyeCurrent Biology, 1999
- A Drosophila Dystrophin-related protein, MSP-300, is required for embryonic muscle morphogenesisMechanisms of Development, 1996
- Crystal Structure of the Repetitive Segments of SpectrinScience, 1993