Characterization of an Importin alpha/beta-recognized nuclear localization signal in beta-dystroglycan (Q24316092)

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Mario Bermúdez de León

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Daniel Leocadio

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Pablo Gómez

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Lizeth Fuentes-Mera

5

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Ivette Martínez-Vieyra

6

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Arturo Ortega

7

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David A Jans

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Bulmaro Cisneros

Journal of Cellular Biochemistry

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language of work or name

English

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publication date

1 June 2010

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published in

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volume

110

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issue

3

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page(s)

706-17

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cites work

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Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins

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Nuclear architecture in the light of gene expression and cell differentiation studies

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Direct interaction of beta-dystroglycan with F-actin

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HIV-1 integrase is capable of targeting DNA to the nucleus via an importin alpha/beta-dependent mechanism.

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Nuclear transport of granzyme B (fragmentin-2). Dependence of perforin in vivo and cytosolic factors in vitro.

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The protein kinase CK2 site (Ser111/112) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin

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Evidence for in situ and in vitro association between beta-dystroglycan and the subsynaptic 43K rapsyn protein. Consequence for acetylcholine receptor clustering at the synapse

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Efficiency of importin alpha/beta-mediated nuclear localization sequence recognition and nuclear import. Differential role of NTF2.

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Edible Mushroom (Agaricus bisporus) Lectin, Which Reversibly Inhibits Epithelial Cell Proliferation, Blocks Nuclear Localization Sequence-dependent Nuclear Protein Import

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Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members

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Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins

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Recruitment of Dbl by ezrin and dystroglycan drives membrane proximal Cdc42 activation and filopodia formation

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