Christopher Surridge

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The TRiC (TCP1 Ring Complex) chaperonin complex participates in the functional folding of actin, centractin, alpha-, beta-, gamma-tubulin, and phytochrome. Each of the cytoskeletal proteins contain a peptide, RK(A,C,T)F/KRAF, located towards the C-terminus, which is homologous to a TCP1 alpha peptide, while the equivalent phytochrome peptide (RLKAF in(More)
Vertebrate beta-tubulins have been classified into six classes on the basis of their C-terminal sequences [(1987) J. Cell Biol. 105, 1707-1720]. In particular, the sequences starting at residue 430 differ between isotypes of the same animal but are conserved between species. We extend this analysis and show that there are three 'hot spots', at residues 35,(More)
The effects of various anionic phospholipids on the in vitro assembly of MAP2/tubulin microtubules has been examined. We show that the potency to inhibit is related to the polarity of the phospholipids and that this is consistent with a mode of action involving the sequencing of microtubule-associated proteins (MAPs) by nonspecific electrostatic(More)
The interactions of bovine brain MAP2 and tau, recombinant murine MAP2C, and recombinant human tau with phosphatidylinositol vesicles yield apparent Kd values of 51 +/- 6 nM, 2.4 +/- 0.6 microM, 1.4 +/- 0.1 microM, and 1.6 +/- 0.2 microM, respectively. Examinations of the binding of MAP2 and/or MAP2C to phosphatidylcholine vesicles doped with(More)
An inhibitor of microtubule assembly has been identified and partially purified from microtubule-depleted brain extracts from day-old chicks and 4-month-old calf. This inhibitor suppresses the self-nucleation of microtubules in vitro with minimal effect upon the final extent of assembly. It may have a developmental role in vivo as it is not detected in(More)