Neutrophil chemoattractant receptors and the membrane skeleton

✍ Scribed by Karl-Norbert Klotz; Algirdas J. Jesaitis

• Book ID: 102761918
• Publisher: John Wiley and Sons
• Year: 1994
• Tongue: English
• Weight: 913 KB
• Volume: 16
• Category: Article
• ISSN: 0265-9247
• DOI: 10.1002/bies.950160310

✦ Synopsis

complement fragment 5a (C5a), leukotriene Bq (LTB4) or platelet-activating factor (PAF), are capable of activating neutrophils via specific receptors. Receptors for N-formyl-Summary 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 a d o r 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 ce11 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.