ArticleProtein science : a publication of the Protein Society2001
Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
11 citing papers in PubMed.
- CaaX-motif adjacent residues control G protein prenylation under suboptimal conditions.bioRxiv : the preprint server for biology · 2023Article
- A model for how Gβγ couples Gα to GPCR.The Journal of general physiology · 2022Article
- Subtype-dependent regulation of Gβγ signalling.Cellular signalling · 2021Review
- Every Detail Matters. That Is, How the Interaction between Gα Proteins and Membrane Affects Their Function.Membranes · 2021Review
- Article
- Gγ identity dictates efficacy of Gβγ signaling and macrophage migration.The Journal of biological chemistry · 2018Article
- Heterotrimeric G-proteins in Picea abies and their regulation in response to Heterobasidion annosum s.l. infection.BMC plant biology · 2015Article
- Diversity of heterotrimeric G-protein γ subunits in plants.BMC research notes · 2012Article
- Central and C-terminal domains of heterotrimeric G protein gamma subunits differentially influence the signaling necessary for primordial germ cell migration.Cellular signalling · 2011Article
- Gamma 2 subunit of G protein heterotrimer is an N-end rule ubiquitylation substrate.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Heterotrimeric and unconventional GTP binding proteins in plant cell signaling.The Plant cell · 2002Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The heterotrimeric GTP binding proteins, G proteins, consist of three distinct subunits: alpha, beta, and gamma. There are 12 known mammalian gamma subunit genes whose products are the smallest and most variable of the G protein subunits. Sequencing of the bovine brain gamma(10) protein by electrospray mass spectrometry revealed that it differs from the human protein by an Ala to Val substitution near the N-terminus. Comparison of gamma isoform subunit sequences indicated that they vary substantially more at the N-terminus than at other parts of the protein. Thus, species variation of this region might reflect the lack of conservation of a functionally unimportant part of the protein. Analysis of 38 gamma subunit sequences from four different species shows that the N-terminus of a given gamma subunit isoform is as conserved between different species as any other part of the protein, including highly conserved regions. These data suggest that the N-terminus of gamma is a functionally important part of the protein exhibiting substantial isoform-specific variation.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.