Menke, Manuela and Gerke, Volker and Steinem, Claudia (2005) Phosphatidylserine membrane domain clustering induced by annexin A2/S100A10 heterotetramer. BIOCHEMISTRY, 44 (46). pp. 15296-15303. ISSN 0006-2960,
Full text not available from this repository. (Request a copy)Abstract
By means of scanning force and fluorescence microscopy of artificial membranes immobilized on mica surfaces, the lateral organization of the annexin A2/S100A10 heterotetramer (annexin A2t) and its influence on the lateral organization of the lipids within the membrane have been elucidated. Planar lipid bilayers composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/1-palmitoyl-2-oleoylsn-glycero-3-phosphoserine (POPS) were prepared on atomically flat mica surfaces by the spreading of unilarnellar vesicles. Fluorescence images of fluorescently labeled annexin A2t and scanning force microscopy images of nonlabeled protein bound to POPC/POPS bilayers show the formation of micrometersized lateral protein domains in the presence of 1 mM CaCl2. By means of scanning force microscopy, not only protein domains became discernible but also small membrane domains, which were attributed to POPS-enriched areas. A depletion of these POPS domains was observed in the vicinity of annexin A2t protein domains. These results indicate that annexin A2t is a peripheral membrane-binding complex capable of inducing lipid segregation.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SOLID-SUPPORTED MEMBRANES; PHOSPHOLIPID MONOLAYERS; RECYCLING ENDOSOMES; LIPID MICRODOMAINS; FORCE MICROSCOPY; BINDING PROTEINS; TYROSINE KINASE; CRYSTAL FORMS; PHOSPHATIDYLCHOLINE; ASSOCIATION; |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Analytische Chemie, Chemo- und Biosensorik |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 23 Apr 2021 06:53 |
| Last Modified: | 23 Apr 2021 06:53 |
| URI: | https://pred.uni-regensburg.de/id/eprint/35410 |
Actions (login required)
 |
View Item |
