Differential localization of unconventional myosin I and nonmuscle myosin II during B cell spreading

Sumoza-Toledo, Adriana; Gillespie, Peter G.; Romero-Ramírez, Héctor; Ferreira-Ishikawa, Hellen C.; Larson, Roy Edward; Santos-Argumedo, Leopoldo

doi:10.1016/j.yexcr.2006.07.002

Cited by 7 publications

(13 citation statements)

References 56 publications

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“…These cells spread onto fibronectin with a time course similar to that of COS7 cells (see below). Consistent with previous reports (Cai et al, 2006;LoRusso et al, 1997;Sumoza-Toledo et al, 2006), we found that both MHC IIA and MHC IIB isoforms localize with FJournal of Cell Science 120 (21) actin in peripheral bundles during cell spreading, although MHC IIA staining was more prominent in A549 cells (Fig. 3a-f).…”

Section: Resultssupporting

confidence: 93%

Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery

Takizawa

Ikebe

et al. 2007

Journal of Cell Science

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Section: Resultssupporting

confidence: 93%

Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery

Takizawa

Ikebe

et al. 2007

Journal of Cell Science

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“…Previous observations from our group indicated that this molecule could be involved in cytoskeleton rearrangements of B lymphocytes, during the spreading induced by immobilized anti-CD44, B220, or MHC-II Abs (17). During livecell observations using GFP tagged Myo1c, we observed strong localization of this molecule in all membrane protrusions generated during spreading in addition to enrichment of the protein at the points where membrane extensions begin to appear.…”

Section: Discussionsupporting

confidence: 56%

“…Previous data from our group showed that Myo1c changes its location pattern in B cells during CD44-induced spreading (17). These observations were limited because of the inability of Ab staining to reveal the dynamic localization of Myo1c in living cells.…”

Section: Myosin 1c Is Localized At Different Membrane Protrusions Of mentioning

confidence: 92%

“…For activation, 2 3 10 6 cells were incubated in 1 ml 10% FBS supplemented RPMI 1640 (Life Technologies) containing LPS from Escherichia coli O55:B5 at 50 mg/ml (Sigma) plus 10 U/ml IL-4 (Genzyme) for 48 h at 37˚C. For immunofluorescence staining, the cells were washed with PBS and fixed for 15 min with 4% paraformaldehyde, permeabilized with 0.1% of Triton X-100, and incubated with different Abs or fluorescent reagents as described previously (17).…”

Section: B Lymphocyte Isolation Activation and Immunofluorescence Smentioning

confidence: 99%

“…We reported previously that mouse B cells express Myo1c (17) and that Myo1g is enriched at the membrane microvilli of human T lymphocytes (18). Given the potential role of class I myosins in regulating cytoskeletal and membrane reorganization, this study investigates the localization of Myo1c during B cell spreading and its possible role during IS formation.…”

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confidence: 97%

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Myosin 1c Participates in B Cell Cytoskeleton Rearrangements, Is Recruited to the Immunologic Synapse, and Contributes to Antigen Presentation

Maravillas-Montero

Gillespie

Patiño-López

et al. 2011

The Journal of Immunology

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Myosin 1c (Myo1c) is a member of the unconventional class I myosins of vertebrates, which directly link the plasma membrane with the microfilament cortical web. Although this molecular motor has been implicated in cell functions such as cytoskeleton organization, cell motility, nuclear transcription, and endocytosis, its role in hematopoietic cells is largely unknown. In this study, we show that Myo1c is abundantly expressed in murine B lymphocytes and is preferentially located at the plasma membrane, especially in peripheral processes such as microvilli. We observed that this motor concentrates at the growing membrane protrusions generated during B cell spreading and that it is actively recruited to the immune synapse. Interestingly, Myo1c was detected in lipid rafts of B cells and showed strong colocalization with MHC-II, particularly after cross-linking of these molecules. By transfection of a dominant negative form of Myo1c or specific siRNA, we also detected alterations in the spreading and Ag-presenting ability of these cells. The data suggest that Myo1c is involved in the cytoskeleton dynamics and membrane protein anchoring or sorting in B lymphocytes.

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Myosin 1g regulates cytoskeleton plasticity, cell migration, exocytosis, and endocytosis in B lymphocytes

et al. 2014

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Myosin 1g (Myo1g) is a hematopoietic-specific myosin expressed mainly by lymphocytes. Here, we report the localization of Myo1g in B-cell membrane compartments such as lipid rafts, microvilli, and membrane extensions formed during spreading. By using Myo1g-deficient mouse B cells, we detected abnormalities in the adhesion ability and chemokineinduced directed migration of these lymphocytes. We also assessed a role for Myo1g in phagocytosis and exocytosis processes, as these were also irregular in Myo1g-deficient B cells. Taken together, our results show that Myo1g acts as a main regulator of different membrane/cytoskeleton-dependent processes in B lymphocytes.Keywords: B lymphocyte r Chemotaxis r Cytoskeleton r Exo-endocytosis r Myosin Additional supporting information may be found in the online version of this article at the publisher's web-site IntroductionMyosin I refers to a class of single-headed and actin-dependent molecular motors, which regulates a number of cellular functions, including intracellular transport, formation of cell-surface projections, regulation of the cytoskeleton, and regulation of membranerelated events, which includes exocytosis, endocytosis, and phagocytosis [1][2][3].Members of myosin I family contain a single heavy chain of 110-140 kDa [4,5], are monomeric, and do not form filaments unlike muscular/conventional myosin II. The single heavy chain is divided into the head (or motor), neck, and tail domains. The motor domain contains the ATP-binding (where ATP is adenosine triphosphate) site and the actin-binding site. This domain is Correspondence: Dr. Leopoldo Santos-Argumedo e-mail: lesantos@cinvestav.mx followed by the neck domain, which is involved in the binding of myosin light chains; molecules identified as calmodulin in vertebrate and yeast class I myosins [6]. Following the neck domain is the C-terminal tail region, which is enriched in basic residues and is involved in the binding of membrane phosphoinositides [7,8]. In humans and mice, eight different genes encode the eight heavy chains of class I myosins and are named Myo1a to Myo1h [2].Myosin 1g (Myo1g) is a vertebrate class I myosin, which is highly represented in leukocytes, according to microarray databases [9][10][11]. Immunoblot analyses of different tissues and cell lines recently identified this protein as being an exclusively hematopoietic motor protein [12,13].Mass spectrometric proteomic profiling of lymphocyte proteins indicates that Myo1g is the most abundant class I myosin * These authors contributed equally to this work. 878José L. Maravillas-Montero et al. Eur. J. Immunol. 2014. 44: 877-886 expressed by T lymphocytes [13]. Immunofluorescence assays showed that Myo1g localizes to the plasma membrane linked to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-triphosphate [14], is particularly enriched at cell-surface microvilli, and associates in an ATP-releasable manner to the actin cytoskeleton [12,13]. In addition to its localization pattern, it has been proposed that this molecula...

show abstract

Differential localization of unconventional myosin I and nonmuscle myosin II during B cell spreading

Cited by 7 publications

References 56 publications

Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery

Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery

Myosin 1c Participates in B Cell Cytoskeleton Rearrangements, Is Recruited to the Immunologic Synapse, and Contributes to Antigen Presentation

Myosin 1g regulates cytoskeleton plasticity, cell migration, exocytosis, and endocytosis in B lymphocytes

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