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  • 1
    Online Resource
    Online Resource
    Informa UK Limited ; 1987
    In:  Molecular and Cellular Biology Vol. 7, No. 11 ( 1987-11-01), p. 3888-3898
    In: Molecular and Cellular Biology, Informa UK Limited, Vol. 7, No. 11 ( 1987-11-01), p. 3888-3898
    Type of Medium: Online Resource
    ISSN: 1098-5549
    Language: English
    Publisher: Informa UK Limited
    Publication Date: 1987
    detail.hit.zdb_id: 1474919-1
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  • 2
    Online Resource
    Online Resource
    The Company of Biologists ; 1998
    In:  Development Vol. 125, No. 20 ( 1998-10-15), p. 3935-3946
    In: Development, The Company of Biologists, Vol. 125, No. 20 ( 1998-10-15), p. 3935-3946
    Abstract: Mutations in the POU domain gene Brn-3c causes hearing impairment in both the human and mouse as a result of inner ear hair cell loss. We show here that during murine embryogenesis, Brn-3c is expressed in postmitotic cells committed to hair cell phenotype but not in mitotic progenitors in the inner ear sensory epithelium. In developing auditory and vestibular sensory epithelia of Brn-3c−/− mice, hair cells are found to be generated and undergo initial differentiation as indicated by their morphology, laminar position and expression of hair cell markers, including myosins VI and VIIa, calretinin and parvalbumin. However, a small number of hair cells are anomalously retained in the supporting cell layer in the vestibular sensory epithelia. Furthermore, the initially differentiated hair cells fail to form stereociliary bundles and degenerate by apoptosis in the Brn-3c−/− mice. These data indicate a crucial role for Brn-3c in maturation, survival and migration of hair cells, but not in proliferation or commitment of hair cell progenitors.
    Type of Medium: Online Resource
    ISSN: 0950-1991 , 1477-9129
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 1998
    detail.hit.zdb_id: 2007916-3
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Informa UK Limited ; 2005
    In:  Molecular and Cellular Biology Vol. 25, No. 11 ( 2005-06-01), p. 4501-4513
    In: Molecular and Cellular Biology, Informa UK Limited, Vol. 25, No. 11 ( 2005-06-01), p. 4501-4513
    Type of Medium: Online Resource
    ISSN: 1098-5549
    Language: English
    Publisher: Informa UK Limited
    Publication Date: 2005
    detail.hit.zdb_id: 1474919-1
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  • 4
    Online Resource
    Online Resource
    The Company of Biologists ; 1994
    In:  Journal of Cell Science Vol. 107, No. 12 ( 1994-12-01), p. 3535-3543
    In: Journal of Cell Science, The Company of Biologists, Vol. 107, No. 12 ( 1994-12-01), p. 3535-3543
    Abstract: Representatives of class V and class VI unconventional myosins are identified as components of the intestinal brush border cytoskeleton. With brush border myosin-I and myosin-II, this brings to four the number of myosin classes associated with this one subcellular domain and represents the first characterization of four classes of myosins expressed in a single metazoan cell type. The distribution and cytoskeletal association of each myosin is distinct as assessed by both biochemical fractionation and immunofluorescence localization. Myosin-VI exists in both the microvillus and terminal web although the terminal web is the predominant site of concentration. Myosin-V is present in the terminal web and, most notably, at the distal ends of the microvilli, thus becoming the first actin-binding protein to be localized to this domain as assessed by both immunohistochemical and biochemical methods. In the undifferentiated enterocytes of the intestinal crypts, myosin-VI is expressed but not yet localized to the brush border, in contrast to myosin-V, which does demonstrate an apical distribution in these cells. An assessment of myosin abundance indicates that while myosin-II is the most abundant in the cell and in the brush border, brush border myosin-I is only slightly less abundant in contrast to myosins-V and -VI, both of which are two orders of magnitude less abundant than the others. Extraction studies indicate that of these four myosins, myosin-V is the most tightly associated with the brush border membrane, as detergent, in addition to ATP, is required for efficient solubilization.
    Type of Medium: Online Resource
    ISSN: 0021-9533 , 1477-9137
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 1994
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    American Society for Cell Biology (ASCB) ; 2015
    In:  CBE—Life Sciences Education Vol. 14, No. 2 ( 2015-06), p. ar12-
    In: CBE—Life Sciences Education, American Society for Cell Biology (ASCB), Vol. 14, No. 2 ( 2015-06), p. ar12-
    Abstract: The 6-yr degree-completion rate of undergraduate science, technology, engineering, and mathematics (STEM) majors at U.S. colleges and universities is less than 40%. Persistence among women and underrepresented minorities (URMs), including African-American, Latino/a, Native American, and Pacific Islander students, is even more troubling, as these students leave STEM majors at significantly higher rates than their non-URM peers. This study utilizes a matched comparison group design to examine the academic achievement and persistence of students enrolled in the Program for Excellence in Education and Research in the Sciences (PEERS), an academic support program at the University of California, Los Angeles, for first- and second-year science majors from underrepresented backgrounds. Results indicate that PEERS students, on average, earned higher grades in most “gatekeeper” chemistry and math courses, had a higher cumulative grade point average, completed more science courses, and persisted in a science major at significantly higher rates than the comparison group. With its holistic approach focused on academics, counseling, creating a supportive community, and exposure to research, the PEERS program serves as an excellent model for universities interested in and committed to improving persistence of underrepresented science majors and closing the achievement gap.
    Type of Medium: Online Resource
    ISSN: 1931-7913
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2015
    detail.hit.zdb_id: 2465176-X
    SSG: 5,3
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  • 6
    Online Resource
    Online Resource
    Wiley ; 2006
    In:  Cell Motility Vol. 63, No. 10 ( 2006-10), p. 633-645
    In: Cell Motility, Wiley, Vol. 63, No. 10 ( 2006-10), p. 633-645
    Abstract: Myosin VI is a minus‐end directed actin‐based molecular motor implicated in uncoated endocytic vesicle transport. Recent kinetic studies have shown that myosin VI displays altered ADP release kinetics under different load conditions allowing myosin VI to serve alternately as a transporter or as an actin tether. We theorized that one potential regulatory event to modulate between these kinetic choices is phosphorylation at a conserved site, threonine 406 (T406) in the myosin VI motor domain. Alterations mimicking the phosphorylated (T406E) and dephosphorylated state (T406A) were introduced into a GFP‐myosin VI fusion (GFP‐M6). Live cell imaging revealed that GFP‐M6(T406E) expression changed the path myosin VI took in its transport of uncoated endocytic vesicles. Rather than routing vesicles inwards as seen in GFP‐M6 and GFP‐M6(T406A) expressing cells, GFP‐M6(T406E) moved vesicles into clusters at distinct peripheral sites. GFP‐M6(T406E) expression also increased the density of the actin cytoskeleton. Filaments were enriched at the vesicle cluster sites. This was not due to a gross redistribution of the actin polymerization machinery. Instead the filament density correlated to the fixed positioning of GFP‐M6(T406E)‐associated vesicles on F‐actin, leading to inhibition of actin depolymerization. Our study suggests that phosphorylation at T406 changes the nature of myosin VI's interaction with actin in vivo. Cell Motil. Cytoskeleton 2006. © 2006 Wiley‐Liss, Inc.
    Type of Medium: Online Resource
    ISSN: 0886-1544
    URL: Issue
    RVK:
    Language: English
    Publisher: Wiley
    Publication Date: 2006
    detail.hit.zdb_id: 2536522-8
    SSG: 12
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  • 7
    In: Nature Genetics, Springer Science and Business Media LLC, Vol. 37, No. 1 ( 2005-1), p. 101-105
    Type of Medium: Online Resource
    ISSN: 1061-4036 , 1546-1718
    RVK:
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2005
    detail.hit.zdb_id: 1494946-5
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    American Society for Cell Biology (ASCB) ; 2003
    In:  Molecular Biology of the Cell Vol. 14, No. 7 ( 2003-07), p. 2728-2743
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 14, No. 7 ( 2003-07), p. 2728-2743
    Abstract: Immunolocalization studies in epithelial cells revealed myo6 was associated with peripherally located vesicles that contained the transferrin receptor. Pulse-chase experiments after transferrin uptake showed that these vesicles were newly uncoated endocytic vesicles and that myo6 was recruited to these vesicles immediately after uncoating. GIPC, a putative myo6 tail binding protein, was also present. Myo6 was not present on early endosomes, suggesting that myo6 has a transient association with endocytic vesicles and is released upon early endosome fusion. Green fluorescent protein (GFP) fused to myo6 as well as the cargo-binding tail (M6tail) alone targeted to the nascent endocytic vesicles. Overexpression of GFP-M6tail had no effect on a variety of organelle markers; however, GFP-M6tail displaced the endogenous myo6 from nascent vesicles and resulted in a significant delay in transferrin uptake. Pulse-chase experiments revealed that transferrin accumulated in uncoated vesicles within the peripheries of transfected cells and that Rab5 was recruited to the surface of these vesicles. Given sufficient time, the transferrin did traffic to the perinuclear sorting endosome. These data suggest that myo6 is an accessory protein required for the efficient transportation of nascent endocytic vesicles from the actin-rich peripheries of epithelial cells, allowing for timely fusion of endocytic vesicles with the early endosome.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2003
    detail.hit.zdb_id: 1474922-1
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    Elsevier BV ; 1999
    In:  Current Biology Vol. 9, No. 22 ( 1999-11), p. R838-R841
    In: Current Biology, Elsevier BV, Vol. 9, No. 22 ( 1999-11), p. R838-R841
    Type of Medium: Online Resource
    ISSN: 0960-9822
    Language: English
    Publisher: Elsevier BV
    Publication Date: 1999
    detail.hit.zdb_id: 2019214-9
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Elsevier BV ; 2001
    In:  Current Opinion in Cell Biology Vol. 13, No. 1 ( 2001-2), p. 29-35
    In: Current Opinion in Cell Biology, Elsevier BV, Vol. 13, No. 1 ( 2001-2), p. 29-35
    Type of Medium: Online Resource
    ISSN: 0955-0674
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2001
    detail.hit.zdb_id: 2013029-6
    SSG: 12
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