The role of a conserved membrane proximal cysteine in altering αPS2CβPS integrin diffusion.

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 Cys¹³⁶⁸ on the diffusion properties of αPS2CβPS integrins are reported. Sequence alignment shows that this cysteine is palmitoylated in human α3 and α6 integrin subunits. Replacing Cys¹³⁶⁸ in wild-type integrins with valine (Val¹³⁶⁸) 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 Val¹³⁶⁸ integrins are more mobile compared to wild-type integrins. Approximately 33% and 8% more Va

SUBMITTER: Syed A 

PROVIDER: S-EPMC5155636 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature