The role of a conserved membrane proximal cysteine in altering α PS2C β PS integrin diffusion
Year: 2016
Type: article
Abstract: Cysteine residues (Cys) in the membrane proximal region are common post-translational modification (PTM) sites in transmembrane proteins. Herein, the effects of a highly conserved membrane proximal α -subunit Cys 1368 on the diffusion properties of α PS2C β PS integrins are reported. Sequence alignment shows that this cysteine is palmitoylated in human α 3 and α 6 integrin subunits. Replacing Cys 1368 in wild-type integrins with valine (Val 1368 ) putatively blocks a PTM site and alters integrins’ ligand binding and diffusion characteristics. Both fluorescence recovery after photobleaching (FRAP) and single particle tracking (SPT) diffusion measurements show Val 1368 integrins are more mobile compared to wild-type integrins. Approximately 33% and 8% more Val 1368 integrins are mobile as measured by FRAP and SPT, respectively. The mobile Val 1368 integrins also exhibit less time-dependent diffusion, as measured by FRAP. Tandem mass spectrometry data suggest that Cys 1368 contains a redox or palmitoylation PTM in α PS2C β PS integrins. This membrane proximal Cys may play an important role in the diffusion of other alpha subunits that contain this conserved residue.
Source: Physical Biology
Authors: Aleem Syed, Neha Arora, Thomas A Bunch, Emily A Smith
Institutions: Iowa State University, University of Arizona
Language: English
Subfield: Immunology and Allergy
Field: Medicine
Domain: Health Sciences
Open Access status: green
Awards: CAREER: Development of Novel Methods to Measure Cell Membrane Protein Clustering in vivo: Unraveling the Relationship between Clustering, Ligand Binding and Cell Signaling, Structure/Function Studies of the Integrin, Uncovering the biophysical mechanism of Receptor for Advanced Glycation Endproducts molecular function
OpenAlex ID: W2551756200