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Cited by 208

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The rod transducin alpha subunit amino terminus is heterogeneously fatty acylated.

Open access
Neubert, T.A., Johnson, R.S., Hurley, J.B., Walsh, K.A.·1992·Journal of Biological Chemistry

Abstract

Rod transducin (Tr), a heterotrimeric GTP-binding protein composed of alpha, beta, and gamma subunits, couples photolysis of rhodopsin to the activation of cyclic GMP phosphodiesterase in the vertebrate visual signal transduction cascade. To determine if T alpha r is covalently modified, we analyzed tryptic fragments of bovine retinal T alpha r using electrospray mass spectrometry, liquid chromatography/mass spectrometry, tandem mass spectrometry, and gas chromatography. A novel heterogeneous fatty acylation was detected at the NH2 terminus. Four types of NH2-terminal tryptic fragments of T alpha r were isolated, and each contained either a lauroyl (C12:0), myristoyl (C14:0), (cis-delta 5)-tetradecaenoyl (C14:1) or (cis,cis-delta 5, delta 8)-tetradecadienoyl (C14:2) fatty acyl residue amide-linked to the NH2-terminal glycine residue. NH2-terminal fatty acylation does not anchor T alpha r permanently in the membrane, since T alpha r used in these experiments was eluted without detergent from rod outer segment membranes.

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Metadata

Authors
Neubert, T. A., Johnson, R. S., Hurley, J. B., & Walsh, K. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-09
Volume
267
Issue
26
Pages
18274-18277
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1494856533
Cited by
208
References
2
FWCI
12.34
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The rod transducin alpha subunit amino terminus is heterogeneously fatty acylated. https://app.cochat.ai/papers/10.1016/s0021-9258(19)36955-8
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Neubert, T. A., Johnson, R. S., Hurley, J. B., & Walsh, K. A. (1992). The rod transducin alpha subunit amino terminus is heterogeneously fatty acylated. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)36955-8

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