Cytoplasmic gamma-tubulin complex from brain contains nonerythroid spectrin
✍ Scribed by Nisha E. Thomas; Sasidharan Shashikala; Suparna Sengupta
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 303 KB
- Volume
- 110
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Abstract
The newer member of the tubulin superfamily, γ‐tubulin, is known to mediate microtubule nucleation from the centrosome of eukaryotic cells with the aid of some other proteins. The major amount of γ‐tubulin is believed to be located in the centrosome before the onset of mitotic division. However, a considerable amount has been found in the cytoplasm in the form of a complex whose function is not well known. Microtubules are most abundant in brain tissues and brain microtubules have been extensively used in many in vitro studies. Thus, it is relevant to use brain tissue to characterize cytoplasmic γ‐tubulin complex. Here we show that cytoplasmic γ‐tubulin in brain tissues exists as a ring complex as in other tissues. Interestingly, along with the common members of the γ‐TuRC reported from several tissues and species, the purified brain cytoplasmic complex contains some high molecular weight proteins including α and β nonerythroid spectrin which are not found in other tissues. Immunohistochemical studies of brain tissue sections also show the co‐localization of γ‐tubulin and spectrin. The possible implications have been discussed. J. Cell. Biochem. 110: 1334–1341, 2010. © 2010 Wiley‐Liss, Inc.
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The presence of g-tubulin in microtubule preparations, obtained by disassembly/ assembly cycles at 0°C/37°C from the brain of several mammals, is demonstrated by immunoblotting with specific antibodies directed against three distinct regions of the protein. In contrast g-tubulin was absent from pure