TY - JOUR
T1 - Sea Anemones, Actinoporins, and Cholesterol
AU - Palacios-Ortega, Juan
AU - Heras-Márquez, Diego
AU - Amigot-Sánchez, Rafael
AU - García-Montoya, Carmen
AU - Torrijos, Carlos
AU - Laxalde, Diego
AU - Gavilanes, José G.
AU - García-Linares, Sara
AU - Martínez-del-Pozo, Álvaro
N1 - Funding Information:
This research was supported by UCM-Banco Santander Grant PR108/20-26896 and by a REACT-EU grant from the Comunidad de Madrid to the ANTICIPA-REACT project of Complutense University of Madrid. This work is also under the auspices of UnaEuropa-2021 (seed funding number SF-2106). J.P.-O. enjoys a post-doctoral research grant from the Magnus Ehrnrooth Foundation. D.H.-M. is a predoctoral fellow from UCM-Banco de Santander CT82/20-CT83/20. The funders had no role in study design, data collection and analysis, preparation of the manuscript or decision to publish.
Publisher Copyright:
© 2022 by the authors.
PY - 2022/8
Y1 - 2022/8
N2 - Spanish or Spanish-speaking scientists represent a remarkably populated group within the scientific community studying pore-forming proteins. Some of these scientists, ourselves included, focus on the study of actinoporins, a fascinating group of metamorphic pore-forming proteins produced within the venom of several sea anemones. These toxic proteins can spontaneously transit from a water-soluble fold to an integral membrane ensemble because they specifically recognize sphingomyelin in the membrane. Once they bind to the bilayer, they subsequently oligomerize into a pore that triggers cell-death by osmotic shock. In addition to sphingomyelin, some actinoporins are especially sensible to some other membrane components such as cholesterol. Our group from Universidad Complutense of Madrid has focused greatly on the role played by sterols in this water–membrane transition, a question which still remains only partially solved and constitutes the main core of the article below.
AB - Spanish or Spanish-speaking scientists represent a remarkably populated group within the scientific community studying pore-forming proteins. Some of these scientists, ourselves included, focus on the study of actinoporins, a fascinating group of metamorphic pore-forming proteins produced within the venom of several sea anemones. These toxic proteins can spontaneously transit from a water-soluble fold to an integral membrane ensemble because they specifically recognize sphingomyelin in the membrane. Once they bind to the bilayer, they subsequently oligomerize into a pore that triggers cell-death by osmotic shock. In addition to sphingomyelin, some actinoporins are especially sensible to some other membrane components such as cholesterol. Our group from Universidad Complutense of Madrid has focused greatly on the role played by sterols in this water–membrane transition, a question which still remains only partially solved and constitutes the main core of the article below.
KW - actinoporins
KW - cholesterol
KW - equinatoxin
KW - fragaceatoxin
KW - pore-forming proteins
KW - sphingomyelin
KW - sticholysin
UR - http://www.scopus.com/inward/record.url?scp=85137085167&partnerID=8YFLogxK
U2 - 10.3390/ijms23158771
DO - 10.3390/ijms23158771
M3 - Review Article or Literature Review
AN - SCOPUS:85137085167
SN - 1661-6596
VL - 23
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 15
M1 - 8771
ER -