Molecular, cellular and physiological aspects of complexes between Gs alpha and tubulin. Witchuda Saengsawang

ISBN: 9781109411232

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105 pages


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Molecular, cellular and physiological aspects of complexes between Gs alpha and tubulin.  by  Witchuda Saengsawang

Molecular, cellular and physiological aspects of complexes between Gs alpha and tubulin. by Witchuda Saengsawang
| NOOKstudy eTextbook | PDF, EPUB, FB2, DjVu, audiobook, mp3, RTF | 105 pages | ISBN: 9781109411232 | 9.34 Mb

Microtubules are a major component of the cytoskeleton. They play a key role in a variety of cellular functions. Microtubules are very dynamic structures and dynamic properties are crucial for cellular there functions.-Signal transduction by GMoreMicrotubules are a major component of the cytoskeleton. They play a key role in a variety of cellular functions. Microtubules are very dynamic structures and dynamic properties are crucial for cellular there functions.-Signal transduction by G proteins is an essential physiological process involved at multiple levels within all living organisms.

G proteins transfer signals from cell surface receptors to intracellular effectors. In addition to this conventional role of the G proteins, the specific G protein alpha subunits have been shown to bind to tubulin with a high affinity (в€ј130 nM) and to have functional effects on tubulin and microtubules. Gsalpha- a stimulatory subunit of G protein, activates the intrinsic tubulin GTPase activity and modulates microtubule assembly and dynamics in vitro . In addition, recent studies have shown that Gsalpha is internalized upon activation.

This activated Gsalpha colocalizes with microtubules and promotes neurite-like outgrowth in PC12 cells and in primary neurons.-This dissertation investigates the role of specific domains of Gsalpha on tubulin and microtubules in order to provide a better understanding of the structure of the Gsalpha-tubulin complex and to explain the physiological interplay between Gsalpha and tubulin.

First, the regions of Gsalpha that interact specifically with tubulin were determined. In addition, Gsalpha-derived peptides from the alpha3-beta5 region were found to stimulate tubulin GTPase activity and therefore to mimic the effect of full length Gsalpha in interactions with tubulin. Moreover, the alpha3-beta5 peptide was also able to increase microtubule dynamics, and especially the catastrophe frequency.

Replacing specific amino acids in alpha3-beta5 peptide by amino acids of transducin (Gtalpha: a G protein that does not bind to tubulin) demonstrates the key role of five amino acid residues for tubulin binding and GTPase activation.

Finally, the conditions used to purify the stable complex of the Gsalpha and tubulin were determined. Collectively, these findings provide a novel insight into structural and physiological details of Gsalpha and tubulin interactions and might provide a tool to probe the interplay between the cytoskeleton and the G protein signaling.



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