%0 Journal Article %1 Jesaitis1993a %A Jesaitis, A. J. %A Klotz, K. N. %D 1993 %J Eur J Haematol %K Acid Actins/*metabolism Amino Cytoskeleton/*physiology Data Formyl GTP-Binding Humans Immunologic/chemistry/*metabolism Molecular Peptide Peptide/chemistry/*metabolism Sequence Signal Transduction Receptor Proteins/metabolism %N 5 %P 288-93 %T Cytoskeletal regulation of chemotactic receptors: molecular complexation of N-formyl peptide receptors with G proteins and actin %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8282090 %V 51 %X 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.

@article{Jesaitis1993a, 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.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Jesaitis, A. J. and Klotz, K. N.}, biburl = {https://www.bibsonomy.org/bibtex/2b1f707265de8e9c324eea8febae3d724/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {2d842571dff1be4aab36daa7ce1e360e}, intrahash = {b1f707265de8e9c324eea8febae3d724}, issn = {0902-4441 (Print) 0902-4441 (Linking)}, journal = {Eur J Haematol}, keywords = {Acid Actins/*metabolism Amino Cytoskeleton/*physiology Data Formyl GTP-Binding Humans Immunologic/chemistry/*metabolism Molecular Peptide Peptide/chemistry/*metabolism Sequence Signal Transduction Receptor Proteins/metabolism}, month = Nov, note = {Jesaitis, A J Klotz, K N 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 Denmark European journal of haematology Eur J Haematol. 1993 Nov;51(5):288-93.}, number = 5, pages = {288-93}, shorttitle = {Cytoskeletal regulation of chemotactic receptors: molecular complexation of N-formyl peptide receptors with G proteins and actin}, timestamp = {2010-12-14T18:21:43.000+0100}, title = {Cytoskeletal regulation of chemotactic receptors: molecular complexation of N-formyl peptide receptors with G proteins and actin}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8282090}, volume = 51, year = 1993 }