Ckap5
- Known as:
- Ckap5
- Catalog number:
- 049506A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Ckap5
Ask about this productRelated genes to: Ckap5
- Gene:
- CKAP5 NIH gene
- Name:
- cytoskeleton associated protein 5
- Previous symbol:
- -
- Synonyms:
- ch-TOG, KIAA0097, TOG, TOGp
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-06-01
- Date modifiied:
- 2014-11-19
Related products to: Ckap5
Related articles to: Ckap5
- The discovery of clathrin was a foundational event in membrane traffic research. Its identification as the major protein component of the coat that surrounds endocytic vesicles kickstarted the biochemical and molecular characterization of endocytosis. During this explosive period of cell biology, there was a parallel storyline involving clathrin which developed more slowly. It emerged that clathrin has an alternative function during mitosis, and that this function is unrelated to its membrane trafficking role. Clathrin forms part of a multiprotein complex that stabilizes microtubules of the mitotic spindle during the chromosome segregation events that occur during cell division. Due to this dual functionality, clathrin is sometimes referred to as a "moonlighting" protein. In this Perspective, we will take a look at this secret life of clathrin and examine how it carries out its mitotic function. - Source: PubMed
Royle Stephen J - It has become increasingly evident in recent years that nucleation of microtubules from a diverse set of microtubule organizing centers (MTOCs) requires both the γ-tubulin ring complex (γ-TuRC) and the microtubule polymerase XMAP215. Despite their essentiality, little is known about how these nucleation factors interact and work together to generate microtubules. Using biochemical domain analysis of XMAP215 and structural approaches, we find that the XMAP215 C-terminal region interacts broadly with γ-TuRC, involving a sixth TOG domain which binds γ-tubulin. Moreover, TOG6 is required for XMAP215 to promote nucleation from γ-TuRC to its full extent. Interestingly, we find that XMAP215 also depends strongly on TOG5 for microtubule lattice binding and nucleation. We further report a cryo-EM structure of TOG5 bound to the microtubule lattice that reveals promotion of lateral interactions between tubulin dimers. While XMAP215 constructs' effects on nucleation are generally proportional to their effects on polymerization, formation of a direct complex with γ-TuRC allows cooperative nucleation activity. Thus, we propose that XMAP215's C-terminal TOGs 5 and 6 play key roles in nucleation by promoting formation of longitudinal and lateral bonds in nascent γ-TuRC-templated microtubules at cellular MTOCs. - Source: PubMed
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