Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.

Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE

Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology

Integrins/*ultrastructure ; Peptides/*genetics ; Receptors, Antigen, T-Cell/*chemistry; Amino Acid Sequence/genetics ; ErbB Receptors/chemistry ; ErbB Receptors/ultrastructure ; Humans ; Integrins/chemistry ; Peptides/chemistry ; Protein Conformation ; Protein Conformation, alpha-Helical/genetics ; Protein Interaction Maps ; Protein Multimerization ; Receptors, Antigen, T-Cell/ultrastructure ; Signal Transduction/genetics

Single-pass membrane receptors contain extracellular domains that respond to external stimuli and transmit information to intracellular domains through a single transmembrane (TM) α-helix. Because membrane receptors have various roles in homeostasis, signaling malfunctions of these receptors can cause disease. Despite their importance, there is still much to be understood mechanistically about how single-pass receptors are activated. In general, single-pass receptors respond to extracellular stimuli via alterations in their oligomeric state. The details of this process are still the focus of intense study, and several lines of evidence indicate that the TM domain (TMD) of the receptor plays a central role. We discuss three major mechanistic hypotheses for receptor activation: ligand-induced dimerization, ligand-induced rotation, and receptor clustering. Recent observations suggest that receptors can use a combination of these activation mechanisms and that technical limitations can bias interpretation. Short peptides derived from receptor TMDs, which can be identified by screening or rationally developed on the basis of the structure or sequence of their targets, have provided critical insights into receptor function. Here, we explore recent evidence that, depending on the target receptor, TMD peptides cannot only inhibit but also activate target receptors and can accommodate novel, bifunctional designs. Furthermore, we call for more sharing of negative results to inform the TMD peptide field, which is rapidly transforming into a suite of unique tools with the potential for future therapeutics.
(© 2020 Westerfield and Barrera.)

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R01 GM120642 United States GM NIGMS NIH HHS

Keywords: T-cell receptor (TCR); cell signaling; conformational change; epidermal growth factor receptor (EGFR); integrin; oligomerization; protein–protein interaction; receptor tyrosine kinase; transmembrane domain; transmembrane receptor; α-helical

PDB 2K9Y; 5EH4

0 (Integrins)
0 (Peptides)
0 (Receptors, Antigen, T-Cell)
EC 2.7.10.1 (EGFR protein, human)
EC 2.7.10.1 (ErbB Receptors)

Date Created: 20191228 Date Completed: 20201014 Latest Revision: 20210329

20231215

PMC7029107

10.1074/jbc.REV119.009457

31879273