RT Journal Article
T1 Molecular dissection of the membrane aggregation mechanisms induced by monomeric annexin A2
A1 López Rodríguez, Juan Carlos
A1 Martínez-Carmona, Francisco
A1 Rodríguez Crespo, José Ignacio
A1 Lizarbe Iracheta, María Antonia
A1 Turnay Abad, Francisco Javier
AB Annexins are a multigene family of proteins involved in aggregation and fusion processes of biological membranes. One of its best-known members is annexin A2 (or p36), capable of binding to acidic phospholipids in a calcium-dependent manner, as occurs with other members of the same family. In its heterotetrameric form, especially with protein S100A10 (p11), annexin A2 has been involved as a determinant factor in innumerable biological processes like tumor development or anticoagulation. However, the subcellular coexistence of different pools of the protein, in which the monomeric form of annexin A2 is growing in functional relevance, is to date poorly described. In this work we present an exhaustive structural and functional characterization of monomeric human annexin A2 by using different recombinant mutants. The important role of the amphipathic N-terminal α-helix in membrane binding and aggregation has been analyzed. We have also studied the potential implication of lateral "antiparallel" protein dimers in membrane aggregation. In contrast to what was previously suggested, formation of these dimers negatively regulate aggregation. We have also confirmed the essential role of three lysine residues located in the convex surface of the molecule in calcium-free and calcium-dependent membrane binding and aggregation. Finally, we propose models for annexin A2-mediated vesicle aggregation mechanisms.
PB Elsevier
SN 0167-4889
YR 2018
FD 2018
LK https://hdl.handle.net/20.500.14352/92362
UL https://hdl.handle.net/20.500.14352/92362
LA eng
NO López-Rodríguez, J. C.; Martínez-Carmona, F. J.; Rodríguez-Crespo, I.; Lizarbe, M. A.; Turnay, J. Molecular dissection of the membrane aggregation mechanisms induced by monomeric annexin A2. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2018, 1865, 863-873 DOI:10.1016/j.bbamcr.2018.03.010.
NO Universidad Complutense de Madrid
DS Docta Complutense
RD 8 abr 2025