ArticleMolecular biology of the cell1998
Plasma membrane localization of G alpha z requires two signals.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 95 citations in OpenAlex.
- From fat to fire: The lipid-inflammasome connection.Immunological reviews · 2025Review
- Recapitulating the potential contribution of protein S-palmitoylation in cancer.Cancer metastasis reviews · 2024Review
- G protein-coupled receptor signaling: transducers and effectors.American journal of physiology. Cell physiology · 2022Review
- Gαi protein subunit: A step toward understanding its non-canonical mechanisms.Frontiers in cell and developmental biology · 2022Review
- Every Detail Matters. That Is, How the Interaction between Gα Proteins and Membrane Affects Their Function.Membranes · 2021Review
- Article
- Effects of Post-translational Modifications on Membrane Localization and Signaling of Prostanoid GPCR-G Protein Complexes and the Role of Hypoxia.The Journal of membrane biology · 2019Review
- Caveolins and cavins in the trafficking, maturation, and degradation of caveolae: implications for cell physiology.American journal of physiology. Cell physiology · 2017Review
- G protein trafficking.Sub-cellular biochemistry · 2012Review
- Site-specific analysis of protein S-acylation by resin-assisted capture.Journal of lipid research · 2011Article
- N-terminal polybasic motifs are required for plasma membrane localization of Galpha(s) and Galpha(q).Cellular signalling · 2008Article
- Cellular palmitoylation and trafficking of lipidated peptides.Journal of lipid research · 2007Article
- Assembly and trafficking of heterotrimeric G proteins.Biochemistry · 2007Review
- Discovery and characterization of inhibitors of human palmitoyl acyltransferases.Molecular cancer therapeutics · 2006Article
- Galpha subunit Gpa2 recruits kelch repeat subunits that inhibit receptor-G protein coupling during cAMP-induced dimorphic transitions in Saccharomyces cerevisiae.Molecular biology of the cell · 2005Article
- Except in every detail: comparing and contrasting G-protein signaling in Saccharomyces cerevisiae and Schizosaccharomyces pombe.Eukaryotic cell · 2005Review
- Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase.Oncogene · 2004Article
- Subcellular targeting of nine calcium-dependent protein kinase isoforms from Arabidopsis.Plant physiology · 2003Article
- Specificity of plasma membrane targeting by the rous sarcoma virus gag protein.Journal of virology · 2003Article
- Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi.Molecular biology of the cell · 2002Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three covalent attachments anchor heterotrimeric G proteins to cellular membranes: the alpha subunits are myristoylated and/or palmitoylated, whereas the gamma chain is prenylated. Despite the essential role of these modifications in membrane attachment, it is not clear how they cooperate to specify G protein localization at the plasma membrane, where the G protein relays signals from cell surface receptors to intracellular effector molecules. To explore this question, we studied the effects of mutations that prevent myristoylation and/or palmitoylation of an epitope-labeled alpha subunit, alpha z. Wild-type alpha z (alpha z-WT) localizes specifically at the plasma membrane. A mutant that incorporates only myristate is mistargeted to intracellular membranes, in addition to the plasma membrane, but transduces hormonal signals as well as does alpha z-WT. Removal of the myristoylation site produced a mutant alpha z that is located in the cytosol, is not efficiently palmitoylated, and does not relay the hormonal signal. Coexpression of beta gamma with this myristoylation defective mutant transfers it to the plasma membrane, promotes its palmitoylation, and enables it to transmit hormonal signals. Pulse-chase experiments show that the palmitate attached to this myristoylation-defective mutant turns over much more rapidly than does palmitate on alpha z-WT, and that the rate of turnover is further accelerated by receptor activation. In contrast, receptor activation does not increase the slow rate of palmitate turnover on alpha z-WT. Together these results suggest that myristate and beta gamma promote stable association with membranes not only by providing hydrophobicity, but also by stabilizing attachment of palmitate. Moreover, palmitoylation confers on alpha z specific localization at the plasma membrane.
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