A family of ras-like GTP-binding proteins expressed in electromotor neurons

Johnny K. Ngsee, Lisa Elferink, Richard H. Scheller

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

The cDNAs encoding seven low molecular weight (LMW) GTP-binding proteins were isolated from an electric lobe library of the marine ray Discopyge ommata. Four were assigned as the ray homologues of previously identified LMW GTP-binding proteins rab1, ral, Krev, and rho. Three others showed unique sequences, including two exhibiting significant similarity to the yeast SEC4 protein. Northern analysis indicated that several of the transcripts are enriched in neural tissues with a moderate level of expression in cardiac muscle. This tissue distribution was corroborated with affinity purified antibodies against the LMW GTP-binding proteins. Subcellular fractionation revealed that the proteins co-purify with cholinergic synaptic vesicles. Immunohistochemical analysis confirms this localization. At least two of the proteins, o-ral and o-rho, are localized to the pre-synaptic terminals.

Original languageEnglish (US)
Pages (from-to)2675-2680
Number of pages6
JournalJournal of Biological Chemistry
Volume266
Issue number4
StatePublished - Feb 5 1991
Externally publishedYes

Fingerprint

ral GTP-Binding Proteins
GTP-Binding Proteins
Neurons
Molecular Weight
Molecular weight
rab1 GTP-Binding Proteins
Tissue
Antibody Affinity
Fungal Proteins
Synaptic Vesicles
Presynaptic Terminals
Tissue Distribution
Fractionation
Cholinergic Agents
Libraries
Muscle
Myocardium
Proteins
Complementary DNA
Antibodies

ASJC Scopus subject areas

  • Biochemistry

Cite this

A family of ras-like GTP-binding proteins expressed in electromotor neurons. / Ngsee, Johnny K.; Elferink, Lisa; Scheller, Richard H.

In: Journal of Biological Chemistry, Vol. 266, No. 4, 05.02.1991, p. 2675-2680.

Research output: Contribution to journalArticle

Ngsee, Johnny K. ; Elferink, Lisa ; Scheller, Richard H. / A family of ras-like GTP-binding proteins expressed in electromotor neurons. In: Journal of Biological Chemistry. 1991 ; Vol. 266, No. 4. pp. 2675-2680.
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