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Moesin and myosin phosphatase confine neutrophil orientation in a chemotactic gradient

Neutrophils respond to invading bacteria by adopting a polarized morphology, migrating in the correct direction, and engulfing the bacteria. How neutrophils establish and precisely orient this polarity toward pathogens remains unclear. Here we report that in resting neutrophils, the ERM (ezrin, radi...

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Detalles Bibliográficos
Autores principales: Liu, Xiaowen, Yang, Tao, Suzuki, Koya, Tsukita, Sachiko, Ishii, Masaru, Zhou, Shuping, Wang, Gang, Cao, Luyang, Qian, Feng, Taylor, Shalina, Oh, Myung-Jin, Levitan, Irena, Ye, Richard D., Carnegie, Graeme K., Zhao, Yong, Malik, Asrar B., Xu, Jingsong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4322047/
https://www.ncbi.nlm.nih.gov/pubmed/25601651
http://dx.doi.org/10.1084/jem.20140508
Descripción
Sumario:Neutrophils respond to invading bacteria by adopting a polarized morphology, migrating in the correct direction, and engulfing the bacteria. How neutrophils establish and precisely orient this polarity toward pathogens remains unclear. Here we report that in resting neutrophils, the ERM (ezrin, radixin, and moesin) protein moesin in its active form (phosphorylated and membrane bound) prevented cell polarization by inhibiting the small GTPases Rac, Rho, and Cdc42. Attractant-induced activation of myosin phosphatase deactivated moesin at the prospective leading edge to break symmetry and establish polarity. Subsequent translocation of moesin to the trailing edge confined the formation of a prominent pseudopod directed toward pathogens and prevented secondary pseudopod formation in other directions. Therefore, both moesin-mediated inhibition and its localized deactivation by myosin phosphatase are essential for neutrophil polarization and effective neutrophil tracking of pathogens.