Intrasubunit Signal Transduction by the Aspartate Chemoreceptor

Receptors that transmit signals across cell membranes are typically composed of multiple subunits. To test whether subunit interactions are required for transmembrane signaling by the bacterial aspartate receptor, dimers were constructed with (i) two full-length subunits, (ii) one full-length subuni...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1991-12, Vol.254 (5038), p.1651-1654
Main Authors: Milligan, Daniel L., Koshland, D. E.
Format: Article
Language:English
Subjects:
Aspartate
Aspartic Acid - physiology
Biochemistry
Cellular biology
Cellular signal transduction
Centrifugation
Dimers
DNA Mutational Analysis
Filtration
Gels
Ligands
Macromolecular Substances
Methylation
Phosphates
Protein Conformation
Receptors
Receptors, Amino Acid
Receptors, Cell Surface - chemistry
Recombinant Proteins
Salmonella typhimurium
Signal Transduction
Sodium
String theory
Structure-Activity Relationship
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Summary:Receptors that transmit signals across cell membranes are typically composed of multiple subunits. To test whether subunit interactions are required for transmembrane signaling by the bacterial aspartate receptor, dimers were constructed with (i) two full-length subunits, (ii) one full-length subunit and one subunit lacking the cytoplasmic domain, or (iii) one full-length subunit and one subunit lacking both the cytoplasmic and the transmembrane domains. Methylation of the cytoplasmic domain of all three receptor constructs was stimulated by the binding of aspartate. These findings demonstrate that transmembrane signaling does not require interactions between cytoplasmic or transmembrane domains of adjacent subunits and suggest that signaling occurs via conformational changes transduced through a single subunit.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1661030