STOP proteins

Cell Structure and Function
C BoscD Job

Abstract

Microtubules assembled from pure tubulin in vitro are labile, rapidly depolymerized upon exposure to the cold. In contrast, in a number of cell types, cytoplasmic microtubules are stable, resistant to prolonged cold exposure. During the past years, the molecular basis of this microtubule stabilization in cells has been elucidated. Cold stability is due to polymer association with different variants of a calmodulin-regulated protein, STOP protein. The dynamic and hence the physiological consequences of STOP association with microtubules vary in different tissues. In neurons, STOP seems almost permanently associated with microtubules. STOP is apparently a major determinant of microtubule turnover in such cells and is required for normal neuronal differentiation. In cycling cells, only minor amounts of STOP are associated with interphase microtubules and STOP does not measurably affects microtubule dynamics. However, STOP is associated with mitotic microtubules in the spindle. Recent results indicate that such an association could be vital for meiosis and for the long-term fidelity of the mitotic process.

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Citations

Mar 31, 2007·Journal of Neuroscience Research·Alice CouégnasNelly Boehm
Dec 8, 2011·Journal of Neurochemistry·Patrick Schloss, Thorsten Lau
Jul 21, 2009·Protist·Antonio Pereira-Neves, Marlene Benchimol
Oct 20, 2006·Journal of Psychopharmacology·Sharon L EastwoodPaul J Harrison
Oct 27, 2011·Anti-cancer Drugs·Luis Miguel Anton AparicioGuadalupe Aparicio Gallego
Feb 13, 2015·Journal of Cell Science·Denis DacheuxMélanie Bonhivers

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