Ontology highlight
ABSTRACT:
SUBMITTER: Guo J
PROVIDER: S-EPMC6261646 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
Guo Jun J Zhang Youhua Y Li Hua H Chu Huiying H Wang Qinshu Q Jiang Shutan S Li Yan Y Shen Hongbin H Li Guohui G Chen Jianfeng J Xu Chenqi C
PLoS biology 20181114 11
Protein transmembrane domains (TMDs) are generally hydrophobic, but our bioinformatics analysis shows that many TMDs contain basic residues at terminal regions. Physiological functions of these membrane-snorkeling basic residues are largely unclear. Here, we show that a membrane-snorkeling Lys residue in integrin αLβ2 (also known as lymphocyte function-associated antigen 1 [LFA-1]) regulates transmembrane heterodimer formation and integrin adhesion through ionic interplay with acidic phospholipi ...[more]