CASK inhibits ECV304 cell growth and interacts with Id1 (Q24294051)

2

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Rongju Sun

3

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Fang Zhang

4

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Xiaofeng Luo

5

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Zongcheng Yang

6

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Xiangdong Luo

Biochemical and Biophysical Research Communications

7

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language of work or name

English

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publication date

11 March 2005

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published in

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volume

328

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issue

2

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page(s)

517-21

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cites work

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Murine CASK is disrupted in a sex-linked cleft palate mouse mutant.

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Mapping and expression analysis of the human CASK gene

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The protein Id: a negative regulator of helix-loop-helix DNA binding proteins

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Differential activity of a variant form of the human Id-1 protein generated by alternative splicing.

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Id proteins in cell growth and tumorigenesis.

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Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2

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Opposing effects of Ets and Id proteins on p16INK4a expression during cellular senescence

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Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila discs large tumor suppressor protein, hDLG, and perturbs its function in cell growth control

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A DNA vector-based RNAi technology to suppress gene expression in mammalian cells

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Characterization of PDZ-binding kinase, a mitotic kinase

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Id1 regulation of cellular senescence through transcriptional repression of p16/Ink4a.

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Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells

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Calcium channel structural determinants of synaptic transmission between identified invertebrate neurons

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Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells

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Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses

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Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein.

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Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins

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CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins

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