Neutrophil chemoattractant receptors and the membrane skeleton
Bioessays, 16 (3):
193-8 (March 1994)Klotz, K N Jesaitis, A J R01 AI22735/AI/NIAID NIH HHS/United States
Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.
Review England BioEssays : news and reviews in molecular, cellular
and developmental biology Bioessays. 1994 Mar;16(3):193-8..Abstract
Signal transduction via receptors for N-formylmethionyl peptide chemoattractants
(FPR) on human neutrophils is a highly regulated process which involves
participation of cytoskeletal-elements. Evidence exists suggesting
that the cytoskeleton and/or the membrane skeleton controls the distribution
of FPR in the plane of the plasma membrane, thus controlling the
accessibility of FPR to different proteins in functionally distinct
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. The mechanism of interaction of FPR with
the membrane skeleton is poorly understood but evidence is accumulating
that suggests a direct binding of FPR (and other receptors) to cytoskeletal
proteins such as actin.