Efficient Front-Rear Coupling in Neutrophil Chemotaxis by Dynamic Myosin II Localization.

Actin Cytoskeleton / metabolism Actins / metabolism Animals Animals, Genetically Modified Cell Line Cell Movement / physiology Cell Polarity / physiology Cell Surface Extensions / physiology Chemotaxis / physiology Cytoskeletal Proteins / metabolism Cytoskeleton / metabolism Female Humans Myosin Type II / metabolism Myosins / metabolism Neutrophils / physiology Zebrafish / metabolism Zebrafish Proteins / metabolism
actin network retrograde flow actin-myosin interaction cell mechanics cell migration cytoskeleton dynamics myosin light chain phosphorylation neutrophil chemotaxis

Journal

Developmental cell
ISSN: 1878-1551
Titre abrégé: Dev Cell
Pays: United States
ID NLM: 101120028

Informations de publication

Date de publication:
22 04 2019
Historique:
received: 18 08 2017
revised: 01 02 2019
accepted: 26 03 2019
entrez: 25 4 2019
pubmed: 25 4 2019
medline: 7 1 2020
Statut: ppublish

Résumé

Efficient chemotaxis requires rapid coordination between different parts of the cell in response to changing directional cues. Here, we investigate the mechanism of front-rear coordination in chemotactic neutrophils. We find that changes in the protrusion rate at the cell front are instantaneously coupled to changes in retraction at the cell rear, while myosin II accumulation at the rear exhibits a reproducible 9-15-s lag. In turning cells, myosin II exhibits dynamic side-to-side relocalization at the cell rear in response to turning of the leading edge and facilitates efficient turning by rapidly re-orienting the rear. These manifestations of front-rear coupling can be explained by a simple quantitative model incorporating reversible actin-myosin interactions with a rearward-flowing actin network. Finally, the system can be tuned by the degree of myosin regulatory light chain (MRLC) phosphorylation, which appears to be set in an optimal range to balance persistence of movement and turning ability.

Identifiants

DOI: 10.1016/j.devcel.2019.03.025 PMID: 31014479 PMC: PMC6708378
pubmed: 31014479
pii: S1534-5807(19)30236-9
doi: 10.1016/j.devcel.2019.03.025
pmc: PMC6708378
mid: NIHMS1046356
pii:
doi:

Substances chimiques

Actins 0
Cytoskeletal Proteins 0
Zebrafish Proteins 0
Myosin Type II EC 3.6.1.-
Myosins EC 3.6.4.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

189-205.e6

Subventions

Organisme : NIGMS NIH HHS
ID : T32 GM007365
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007276
Pays : United States
Organisme : NIGMS NIH HHS
ID : P50 GM107615
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM046383
Pays : United States
Organisme : NIH HHS
ID : S10 OD018073
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM074827
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM092804
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131792
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM127026
Pays : United States
Organisme : NIBIB NIH HHS
ID : P41 EB002503
Pays : United States

Informations de copyright

Copyright © 2019 Elsevier Inc. All rights reserved.

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Auteurs

Tony Y-C Tsai (TY)

Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, USA; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA; Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA.

Sean R Collins (SR)

Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, USA.

Caleb K Chan (CK)

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA; Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA.

Amalia Hadjitheodorou (A)

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA; Department of Bioengineering, Stanford University School of Medicine, Stanford, CA, USA; Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA.

Pui-Ying Lam (PY)

Department of Pediatrics and Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA; Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, WI 53706, USA.

Sunny S Lou (SS)

Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, USA; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA; Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA.

Hee Won Yang (HW)

Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, USA.

Julianne Jorgensen (J)

Department of Surgery, BioMEMS Resource Center, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02129, USA.

Felix Ellett (F)

Department of Surgery, BioMEMS Resource Center, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02129, USA.

Daniel Irimia (D)

Department of Surgery, BioMEMS Resource Center, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02129, USA.

Michael W Davidson (MW)

National High Magnetic Field Laboratory, Department of Biological Science, The Florida State University, Tallahassee, FL 32304, USA.

Robert S Fischer (RS)

National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

Anna Huttenlocher (A)

Department of Pediatrics and Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA.

Tobias Meyer (T)

Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, USA.

James E Ferrell (JE)

Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, USA; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA.

Julie A Theriot (JA)

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA; Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: jtheriot@uw.edu.

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Classifications MeSH

questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Cytosquelette › Cytosquelette d'actine › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Protéines des microfilaments › Actines › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Eucaryotes › Animaux › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Stades d'organismes › Organismes génétiquement modifiés › Animal génétiquement modifié › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Cellules › Cellules cultivées › Lignée cellulaire › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Phénomènes physiologiques › Mouvement cellulaire › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Polarité de la cellule › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Cellules › Structures cellulaires › Prolongements cytoplasmiques › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Phénomènes physiologiques de l'appareil locomoteur et du système nerveux › Phénomènes physiologiques du système locomoteur › Mouvement › Locomotion › Taxie › Chimiotaxie › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Cytosquelette › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Protéines des microfilaments › Myosines › Myosine de type II › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Protéines des microfilaments › Myosines › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Systèmes sanguin et immunitaire › Système immunitaire › Phagocytes › Granulocytes neutrophiles › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Poissons › Cypriniformes › Cyprinidae › Danio zébré › Efficient Front-Rear Coupling in Neutrophil...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de poisson › Protéines de poisson-zèbre › Efficient Front-Rear Coupling in Neutrophil...