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TitleStructural basis for the extended CAP-Gly domains of p150(glued) binding to microtubules and the implication for tubulin dynamics.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 111, Issue 31, Page 11347-11352, Year 2014
Publish dateAug 5, 2014
AuthorsQianmin Wang / Alvaro H Crevenna / Ines Kunze / Naoko Mizuno /
PubMed Abstractp150(glued) belongs to a group of proteins accumulating at microtubule plus ends (+TIPs). It plays a key role in initiating retrograde transport by recruiting and tethering endosomes and dynein to ...p150(glued) belongs to a group of proteins accumulating at microtubule plus ends (+TIPs). It plays a key role in initiating retrograde transport by recruiting and tethering endosomes and dynein to microtubules. p150(glued) contains an N-terminal microtubule-binding cytoskeleton-associated protein glycine-rich (CAP-Gly) domain that accelerates tubulin polymerization. Although this copolymerization is well-studied using light microscopic techniques, structural consequences of this interaction are elusive. Here, using electron-microscopic and spectroscopic approaches, we provide a detailed structural view of p150(glued) CAP-Gly binding to microtubules and tubulin. Cryo-EM 3D reconstructions of p150(glued)-CAP-Gly complexed with microtubules revealed the recognition of the microtubule surface, including tubulin C-terminal tails by CAP-Gly. These binding surfaces differ from other retrograde initiation proteins like EB1 or dynein, which could facilitate the simultaneous attachment of all accessory components. Furthermore, the CAP-Gly domain, with its basic extensions, facilitates lateral and longitudinal interactions of tubulin molecules by covering the tubulin acidic tails. This shielding effect of CAP-Gly and its basic extensions may provide a molecular basis of the roles of p150(glued) in microtubule dynamics.
External linksProc Natl Acad Sci U S A / PubMed:25059720 / PubMed Central
MethodsEM (helical sym.)
Resolution9.7 - 12.0 Å
Structure data

EMDB-2673:
Cryo-EM map of CAP-Gly-microtubule complex
Method: EM (helical sym.) / Resolution: 9.7 Å

EMDB-2674:
Cryo-EM map of p150 CAP-Gly-microtubule complex
Method: EM (helical sym.) / Resolution: 9.7 Å

EMDB-2675:
Cryo-EM map of CAP-Gly-microtubule complex
Method: EM (helical sym.) / Resolution: 12.0 Å

Source
  • Homo sapiens (human)

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