Crystal structures of IFT70/52 and IFT52/46 provide insight into intraflagellar transport B core complex assembly
نویسندگان
چکیده
منابع مشابه
Crystal structures of IFT70/52 and IFT52/46 provide insight into intraflagellar transport B core complex assembly
Cilia are microtubule-based organelles that assemble via intraflagellar transport (IFT) and function as signaling hubs on eukaryotic cells. IFT relies on molecular motors and IFT complexes that mediate the contacts with ciliary cargo. To elucidate the architecture of the IFT-B complex, we reconstituted and purified the nonameric IFT-B core from Chlamydomonas reinhardtii and determined the cryst...
متن کاملDissecting the Sequential Assembly and Localization of Intraflagellar Transport Particle Complex B in Chlamydomonas
Intraflagellar transport (IFT), the key mechanism for ciliogenesis, involves large protein particles moving bi-directionally along the entire ciliary length. IFT particles contain two large protein complexes, A and B, which are constructed with proteins in a core and several peripheral proteins. Prior studies have shown that in Chlamydomonas reinhardtii, IFT46, IFT52, and IFT88 directly interac...
متن کاملCrystal structure of the intraflagellar transport complex 25/27.
The cilium is an important organelle that is found on many eukaryotic cells, where it serves essential functions in motility, sensory reception and signalling. Intraflagellar transport (IFT) is a vital process for the formation and maintenance of cilia. We have determined the crystal structure of Chlamydomonas reinhardtii IFT25/27, an IFT sub-complex, at 2.6 Å resolution. IFT25 and IFT27 intera...
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PGAM5 is a mitochondrial membrane protein that functions as an atypical Ser/Thr phosphatase and is a regulator of oxidative stress response, necroptosis, and autophagy. Here we present several crystal structures of PGAM5 including the activating N-terminal regulatory sequences, providing a model for structural plasticity, dimerization of the catalytic domain, and the assembly into an enzymatica...
متن کاملRABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
Proteins localized to the basal body and the centrosome play crucial roles in ciliary assembly and function. Although RABL2 and CEP19 are conserved in ciliated organisms and have been implicated in ciliary/flagellar functions, their roles are poorly understood. Here we show that RABL2 interacts with CEP19 and is recruited to the mother centriole and basal body in a CEP19-dependent manner and th...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2014
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.201408002