DOI: 10.1091/mbc.9.1.1. Plasma Membrane Localization of Gα<sub>z</sub>Requires Two Signals

Plasma Membrane Localization of GαzRequires Two Signals

10.1091/mbc.9.1.1

Crossref journal-article

American Society for Cell Biology (ASCB)

Molecular Biology of the Cell (1076)

Abstract

Three covalent attachments anchor heterotrimeric G proteins to cellular membranes: the α subunits are myristoylated and/or palmitoylated, whereas the γ 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 α subunit, αz. Wild-type αz(αz-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 αz-WT. Removal of the myristoylation site produced a mutant αzthat is located in the cytosol, is not efficiently palmitoylated, and does not relay the hormonal signal. Coexpression of βγ 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 αz-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 αz-WT. Together these results suggest that myristate and βγ promote stable association with membranes not only by providing hydrophobicity, but also by stabilizing attachment of palmitate. Moreover, palmitoylation confers on αzspecific localization at the plasma membrane.

Bibliography

Morales, J., Fishburn, C. S., Wilson, P. T., & Bourne, H. R. (1998). Plasma Membrane Localization of GÎ±zRequires Two Signals. Molecular Biology of the Cell, 9(1), 1â14.

Authors 4

Janine Morales (first)
C. Simone Fishburn (additional)
Paul T. Wilson (additional)
Henry R. Bourne (additional)

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Dates

Type	When
Created	12 years, 1 month ago (July 2, 2013, 7:12 p.m.)
Deposited	3 years, 6 months ago (Feb. 26, 2022, 9:34 p.m.)
Indexed	1 week, 1 day ago (Aug. 19, 2025, 6:26 a.m.)
Issued	27 years, 7 months ago (Jan. 1, 1998)
Published	27 years, 7 months ago (Jan. 1, 1998)
Published Print	27 years, 7 months ago (Jan. 1, 1998)

Funders 0

None

BibTeX

@article{Morales_1998, title={Plasma Membrane Localization of GαzRequires Two Signals}, volume={9}, ISSN={1939-4586}, url={http://dx.doi.org/10.1091/mbc.9.1.1}, DOI={10.1091/mbc.9.1.1}, number={1}, journal={Molecular Biology of the Cell}, publisher={American Society for Cell Biology (ASCB)}, author={Morales, Janine and Fishburn, C. Simone and Wilson, Paul T. and Bourne, Henry R.}, year={1998}, month=jan, pages={1–14} }

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  "abstract": "<jats:p>Three covalent attachments anchor heterotrimeric G proteins to cellular membranes: the \u03b1 subunits are myristoylated and/or palmitoylated, whereas the \u03b3 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 \u03b1 subunit, \u03b1<jats:sub>z</jats:sub>. Wild-type \u03b1<jats:sub>z</jats:sub>(\u03b1<jats:sub>z</jats:sub>-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 \u03b1<jats:sub>z</jats:sub>-WT. Removal of the myristoylation site produced a mutant \u03b1<jats:sub>z</jats:sub>that is located in the cytosol, is not efficiently palmitoylated, and does not relay the hormonal signal. Coexpression of \u03b2\u03b3 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 \u03b1<jats:sub>z</jats:sub>-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 \u03b1<jats:sub>z</jats:sub>-WT. Together these results suggest that myristate and \u03b2\u03b3 promote stable association with membranes not only by providing hydrophobicity, but also by stabilizing attachment of palmitate. Moreover, palmitoylation confers on \u03b1<jats:sub>z</jats:sub>specific localization at the plasma membrane.</jats:p>",
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