Adhesion GPCRs as a putative class of metabotropic mechanosensors

Nicole Scholz, Kelly R. Monk, Robert J. Kittel, Tobias Langenhan

Research output: Chapter in Book/Report/Conference proceedingChapter

46 Scopus citations

Abstract

G protein-coupled receptors (GPCRs) constitute the most versatile superfamily of biosensors. This group of receptors is formed by hundreds of GPCRs, each of which is tuned to the perception of a specific set of stimuli a cell may encounter emanating from the outside world or from internal sources. Most GPCRs are receptive for chemical compounds such as peptides, proteins, lipids, nucleotides, sugars, and other organic compounds, and this capacity is utilized in several sensory organs to initiate visual, olfactory, gustatory, or endocrine signals. In contrast, GPCRs have only anecdotally been implicated in the perception of mechanical stimuli. Recent studies, however, show that the family of adhesion GPCRs (aGPCRs), which represents a large panel of over 30 homologs within the GPCR superfamily, displays molecular design and expression patterns that are compatible with receptivity toward mechanical cues (Fig. 1). Here, we review physiological and molecular principles of established mechanosensors, discuss their relevance for current research of the mechanosensory function of aGPCRs, and survey the current state of knowledge on aGPCRs as mechanosensing molecules.

Original languageEnglish (US)
Title of host publicationHandbook of Experimental Pharmacology
PublisherSpringer New York LLC
Pages221-247
Number of pages27
DOIs
StatePublished - Nov 1 2016
Externally publishedYes

Publication series

NameHandbook of Experimental Pharmacology
Volume234
ISSN (Print)0171-2004
ISSN (Electronic)1865-0325

Keywords

  • Adhesion GPCR
  • Mechanosensation
  • Mechanosensor

ASJC Scopus subject areas

  • General Pharmacology, Toxicology and Pharmaceutics
  • Biochemistry

Fingerprint

Dive into the research topics of 'Adhesion GPCRs as a putative class of metabotropic mechanosensors'. Together they form a unique fingerprint.

Cite this