Autor: |
Kamlesh K, Gupta, Emily O, Alberico, Inke S, Näthke, Holly V, Goodson |
Rok vydání: |
2014 |
Předmět: |
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Zdroj: |
BioEssays : news and reviews in molecular, cellular and developmental biology. 36(9) |
ISSN: |
1521-1878 |
Popis: |
Regulation of microtubule (MT) dynamics is essential for many cellular processes, but the machinery that controls MT dynamics remains poorly understood. MT plus-end tracking proteins (+TIPs) are a set of MT-associated proteins that dynamically track growing MT ends and are uniquely positioned to govern MT dynamics. +TIPs associate with each other in a complex array of inter- and intra-molecular interactions known as the "+TIP network." Why do so many +TIPs bind to other +TIPs? Typical answers include the ideas that these interactions localize proteins where they are needed, deliver proteins to the cortex, and/or create regulatory pathways. We propose an additional and more mechanistic hypothesis: that +TIPs bind each other to create a superstructure that promotes MT assembly by constraining the structural fluctuations of the MT tip, thus acting as a polymerization chaperone. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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