Please use this identifier to cite or link to this item:
http://hdl.handle.net/20.500.11889/5423
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sarkar-Banerjee, Suparna | |
dc.contributor.author | Sayyed-Ahmad, Abdallah | |
dc.contributor.author | Prakash, Priyanka | |
dc.contributor.author | Cho, Kwang-Jin | |
dc.contributor.author | Waxham, Neal | |
dc.contributor.author | Hancock, John F. | |
dc.contributor.author | Gorfe, Alemayehu | |
dc.date.accessioned | 2018-03-12T06:12:40Z | |
dc.date.available | 2018-03-12T06:12:40Z | |
dc.date.issued | 2017-09-01 | |
dc.identifier.citation | Sarkar-Banerjee S, Sayyed-Ahmad A, Prakash P, Cho KJ, Waxham MN, Hancock JF, and Gorfe AA “Spatiotemporal analysis of K-Ras plasma membrane interactions reveals multiple high order homo-oligomeric complexes”, Journal of American Chemical Society, 2017, 139 (38), pp 13466–13475 | en_US |
dc.identifier.uri | http://hdl.handle.net/20.500.11889/5423 | |
dc.description | An Article published in : Journal of American Chemical Society, 2017, 139 (38), pp. 13466–13475 | |
dc.description.abstract | Self-assembly of plasma membrane-associated Ras GTPases has major implications to the regulation of cell signaling. However, the structural basis of homo-oligomerization and the fractional distribution of oligomeric states remained undetermined. We have addressed these issues by deciphering the distribution of dimers and higher-order oligomers of K-Ras4B, the most frequently mutated Ras isoform in human cancers. We focused on the constitutively active G12V K-Ras and two of its variants, K101E and K101C/E107C, which respectively destabilize and stabilize oligomers. Using raster image correlation spectroscopy and number and brightness analysis combined with fluorescence recovery after photobleaching, fluorescence correlation spectroscopy and electron microscopy in live cells, we show that G12V K-Ras exists as a mixture of monomers, dimers and larger oligomers, while the K101E mutant is predominantly monomeric and K101C/E107C is dominated by oligomers. This observation demonstrates the ability of K-Ras to exist in multiple oligomeric states whose population can be altered by interfacial mutations. Using molecular modeling and simulations we further show that K-Ras uses two partially overlapping interfaces to form compositionally and topologically diverse oligomers. Our results thus provide the first detailed insight into the multiplicity, structure, and membrane organization of K-Ras homomers. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | ACS | en_US |
dc.subject | K-Ras | en_US |
dc.subject | Ras oncogenes | en_US |
dc.subject.lcsh | GTPase-activating protein | |
dc.subject.lcsh | Oligomerization | |
dc.subject.lcsh | Mutation (Biology) | |
dc.subject.lcsh | Cell membranes - Electric properties | |
dc.title | Spatiotemporal analysis of K-Ras plasma membrane interactions reveals multiple high order homo-oligomeric complexes | en_US |
dc.type | Article | en_US |
newfileds.department | Science | en_US |
newfileds.item-access-type | bzu | en_US |
newfileds.thesis-prog | none | en_US |
newfileds.general-subject | Natural Sciences | العلوم الطبيعية | en_US |
item.fulltext | With Fulltext | - |
item.grantfulltext | open | - |
item.languageiso639-1 | other | - |
Appears in Collections: | Fulltext Publications |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Sayyed 1 Spatiotemporal.pdf | 5.65 MB | Adobe PDF | View/Open |
Page view(s)
133
Last Week
0
0
Last month
2
2
checked on Apr 14, 2024
Download(s)
25
checked on Apr 14, 2024
Google ScholarTM
Check
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.