Two intracellular helices of G-protein coupling receptors could generally support oligomerization and coupling with transducers

Michael S. Parker, Edwards Park, Floyd R. Sallee, Steven L. Parker

Research output: Contribution to journalReview article

7 Citations (Scopus)

Abstract

For many G-protein coupling receptors (GPCRs), the upkeep of receptor dimers could depend on association with functional Gi α subunits. This is known for Y1, Y2 and Y4 neuropeptide Y receptors [presented in the companion paper (Estes et al., Amino Acids, doi: 10.1007/s00726-010-0642-z, 2010)]. Interactions with transducers use mainly intracellular domains of the receptors. Intracellular loops 1 and 2 in GPCRs are short and lack extensive helicity that could support transducer anchoring. Interaction with G-proteins is known to use the juxtamembrane Helix 8 in the fourth intracellular domain, for which we document a helix-stabilizing n/(n + 4) pattern of large hydrophobic sidechains. Another intracellular helix located in the C-terminal portion of the third intracellular loop does not display a strong stabilizing pattern, and is found in many studies to serve dynamically in association and activation of transducers and effectors. We show that these tracts share features across metazoan phyla not only in opsins and opsin-like receptors (including the Y receptors), but also in Taste-2 and Frizzled receptors. Similarities of these helices across GPCR groups could have both phylogenetic and functional roots.

Original languageEnglish (US)
Pages (from-to)261-268
Number of pages8
JournalAmino Acids
Volume40
Issue number2
DOIs
StatePublished - Feb 1 2011

Fingerprint

Oligomerization
Transducers
GTP-Binding Proteins
Opsins
Association reactions
Frizzled Receptors
Neuropeptide Y Receptors
Dimers
Chemical activation
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

Cite this

Two intracellular helices of G-protein coupling receptors could generally support oligomerization and coupling with transducers. / Parker, Michael S.; Park, Edwards; Sallee, Floyd R.; Parker, Steven L.

In: Amino Acids, Vol. 40, No. 2, 01.02.2011, p. 261-268.

Research output: Contribution to journalReview article

Parker, Michael S. ; Park, Edwards ; Sallee, Floyd R. ; Parker, Steven L. / Two intracellular helices of G-protein coupling receptors could generally support oligomerization and coupling with transducers. In: Amino Acids. 2011 ; Vol. 40, No. 2. pp. 261-268.
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