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      Confinement-Optimized 3-Dimensional T cell Amoeboid Motility is Modulated via Myosin IIA-Regulated Adhesions

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          Abstract

          During trafficking through tissues, T cells fine-tune their motility to balance the extent and duration of cell-surface contacts with the need to traverse an entire organ. In vivo, Myosin-IIA-deficient T cells exhibited a triad of defects including over-adherence to high-endothelial venules, reduced interstitial migration, and inefficient completion of recirculation through lymph nodes. Spatiotemporal analysis of 3-dimensional motility in microchannels revealed that the degree of confinement and Myosin-IIA function, rather than integrin adhesion as proposed by the haptokinetic model, optimize motility rate. This occurs via a Myosin-IIA-dependent rapid ‘walking’ motility mode using multiple small and simultaneous adhesions to the substrate, which prevent spurious and prolonged adhesions. Adhesion discrimination provided by Myosin-IIA is thus necessary for optimizing motility through complex tissues.

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          Non-muscle myosin II takes centre stage in cell adhesion and migration.

          Miguel Vicente-Manzanares, Xuefei Ma, Robert S Adelstein … (2009)
          Non-muscle myosin II (NM II) is an actin-binding protein that has actin cross-linking and contractile properties and is regulated by the phosphorylation of its light and heavy chains. The three mammalian NM II isoforms have both overlapping and unique properties. Owing to its position downstream of convergent signalling pathways, NM II is central in the control of cell adhesion, cell migration and tissue architecture. Recent insight into the role of NM II in these processes has been gained from loss-of-function and mutant approaches, methods that quantitatively measure actin and adhesion dynamics and the discovery of NM II mutations that cause monogenic diseases.
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            Cellular motility driven by assembly and disassembly of actin filaments.

            Thomas Pollard, Gary Borisy (2003)
            Motile cells extend a leading edge by assembling a branched network of actin filaments that produces physical force as the polymers grow beneath the plasma membrane. A core set of proteins including actin, Arp2/3 complex, profilin, capping protein, and ADF/cofilin can reconstitute the process in vitro, and mathematical models of the constituent reactions predict the rate of motion. Signaling pathways converging on WASp/Scar proteins regulate the activity of Arp2/3 complex, which mediates the initiation of new filaments as branches on preexisting filaments. After a brief spurt of growth, capping protein terminates the elongation of the filaments. After filaments have aged by hydrolysis of their bound ATP and dissociation of the gamma phosphate, ADF/cofilin proteins promote debranching and depolymerization. Profilin catalyzes the exchange of ADP for ATP, refilling the pool of ATP-actin monomers bound to profilin, ready for elongation.
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              Stromal cell networks regulate lymphocyte entry, migration, and territoriality in lymph nodes.

              Marc Bajénoff, Jackson G Egen, Lily Y. Koo … (2006)
              After entry into lymph nodes (LNs), B cells migrate to follicles, whereas T cells remain in the paracortex, with each lymphocyte type showing apparently random migration within these distinct areas. Other than chemokines, the factors contributing to this spatial segregation and to the observed patterns of lymphocyte movement are poorly characterized. By combining confocal, electron, and intravital microscopy, we showed that the fibroblastic reticular cell network regulated naive T cell access to the paracortex and also supported and defined the limits of T cell movement within this domain, whereas a distinct follicular dendritic cell network similarly served as the substratum for movement of follicular B cells. These results highlight the central role of stromal microanatomy in orchestrating cell migration within the LN.
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                Author and article information

                Journal
                Journal ID (nlm-journal-id): 100941354
                Journal ID (pubmed-jr-id): 21750
                Journal ID (nlm-ta): Nat Immunol
                Title: Nature immunology
                ISSN (Print): 1529-2908
                ISSN (Electronic): 1529-2916
                Publication date Nihms-submitted: 25 August 2010
                Publication date (Electronic): 12 September 2010
                Publication date (Print): October 2010
                Publication date PMC-release: 1 April 2011
                Volume: 11
                Issue: 10
                Pages: 953-961
                Affiliations
                [1 ]Department of Pathology; University of California San Francisco. 513 Parnassus Avenue HSW-0511, San Francisco CA 94143 USA.
                [2 ]Laboratory of Molecular Cardiology; National Heart, Lung and Blood Institute, NIH, 10 Center Drive MSC-1583, Bethesda, MD 20892, USA.
                [3 ]INSERM U653, Institut Curie, 12 Rue Lhomond, 75005, Paris, France.
                Author notes
                Correspondence should be addressed to M.F.K. ( matthew.krummel@ 123456ucsf.edu )
                Article
                Manuscript ID: nihpa229577
                DOI: 10.1038/ni.1936
                PMC ID: 2943564
                PubMed ID: 20835229
                SO-VID: ccaa7130-24c6-415e-a14e-ae3c813bc8d5
                License:

                Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms

                History
                Funding
                Funded by: National Institute of Allergy and Infectious Diseases Extramural Activities : NIAID
                Award ID: R01 AI052116-07 ||AI
                Categories
                Subject: Article

                ScienceOpen disciplines: Immunology
                Keywords: adhesion,t cells,myosin-iia,cytoskeleton,motility
                Data availability:
                ScienceOpen disciplines: Immunology
                Keywords: adhesion, t cells, myosin-iia, cytoskeleton, motility

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