Cytoskeletal regulation of chemotactic receptors: molecular complexation of N-formyl peptide receptors with G proteins and actin.

Abstract:

:Signal transduction via receptors for N-formylmethionyl peptide chemoattractants (FPR) on human neutrophils is a highly regulated process. It involves direct interaction of receptors with heterotrimeric G-proteins and may be under the control of cytoskeletal elements. Evidence exists suggesting that the cytoskeleton and/or the membrane skeleton determines the distribution of FPR in the plane of the plasma membrane, thus controlling FPR accessibility to different proteins in functionally distinct membrane domains. In desensitized cells, FPR are restricted to domains which are depleted of G proteins but enriched in cytoskeletal proteins such as actin and fodrin. Thus, the G protein signal transduction partners of FPR become inaccessible to the agonist-occupied receptor, preventing cell activation. We are investigating the molecular basis for the interaction of FPR with the membrane skeleton, and our results suggest that FPR, and possibly other receptors, may directly bind to cytoskeletal proteins such as actin.

journal_name

Eur J Haematol

authors

Jesaitis AJ,Klotz KN

doi

10.1111/j.1600-0609.1993.tb01610.x

subject

Has Abstract

pub_date

1993-11-01 00:00:00

pages

288-93

issue

5

eissn

0902-4441

issn

1600-0609

journal_volume

51

pub_type

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