ISSN:
0886-1544
Keywords:
microtubule
;
tubulin
;
MAPs
;
calcium
;
mitosis
;
unfertilized sea urchin egg
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Medicine
Notes:
Cytoplasmic tubulin purified from unfertilized sea urchin eggs self-assembles in the absence of microtubule-associated proteins (MAPs) [Suprenant and Rebhun, 1983; Detrich and Wilson, 1983] with a critical concentration for polymerization of 0.8 mg/ml at 15-18°C, a value well below the 3 mg/ml tubulin present in these eggs [Pfeffer et al, 1976]. Studies of the calcium sensitivity of unfertilized S. purpuratus (sea urchin) egg tubulin were initiated to help understand how this tubulin is maintained unassembled in the unfertilized egg. Egg microtubules, assembled at physiological temperatures (15-18°C) were depolymerized by a 100-fold lower free calcium concentration than egg microtubules assembled at the higher temperatures (25-37°C) generally used to assemble mammalian brain microtubules. The initial rate of egg microtubule assembly was much more sensitive to calcium than was microtubule depolymerization at steady state at 37°C. However, both processes were sensitive to near physiological free calcium of free calcium for depolymerization than microtubules assembled at 18°C from egg tubulin alone. While calcium regulatory MAPs have not yet been found in sea urchin eggs, the fact that brain MAPs interact with egg tubulin and regulate both its critical concentration for polymerization [Suprenant and Rebhun, 1983] and its calcium sensitivty, suggests that such regulatory molecules exist. These results suggest that sea urchin egg tubulin assembly in vivo could be controlled by variations in interacellular calcium levels acting in concert with urchin egg proteins similar in function to brain MAPs.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/cm.970040504
Permalink
