Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP.

Haffner, Christof; Jarchau, Thomas; Reinhard, Matthias; Hoppe, Jürgen; Lohmann, Suzanne M.; Walter, Ulrich

doi:10.1002/j.1460-2075.1995.tb06971.x

Cited by 198 publications

(171 citation statements)

References 45 publications

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“…The N-terminal 110 amino acid residues of Homer proteins share sequence and secondary structure similarity with (a) the Ena/VASP homology domain 1 (EVH1 domain) of the Enabled protein of Drosophila (Ena) (18), (b) the vasodilator-stimulated phosphoprotein (VASP) (19,20), and (c) the Ran-binding protein family (21). All these proteins have been implicated in binding to proline-rich domains of various cytoskeletal proteins.…”

Section: Homer Protein Structurementioning

confidence: 99%

Homer/Vesl Proteins and Their Roles in CNS Neurons

Ehrengruber

Kato

Inokuchi

et al. 2004

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Section: Homer Protein Structurementioning

confidence: 99%

Homer/Vesl Proteins and Their Roles in CNS Neurons

Ehrengruber

Kato

Inokuchi

et al. 2004

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“…Colocalization of VASP with Attached H. pylori. VASP is a known substrate for both cAMP-and cGMP-dependent protein kinases (27), placing VASP phosphorylation at the junction of two signal transduction pathways. VASP and profilin, which bind in vivo (28,29), appear to act conjointly to relay signal transduction to the actin cytoskeleton.…”

Section: H Pylori Attachment To Cultured Gastric Epithelial Cellsmentioning

confidence: 99%

Induction of host signal transduction pathways by Helicobacter pylori

Segal

Lange

Covacci

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

187

153

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Adherence of Helicobacter pylori to cultured gastric epithelial cells is associated with several cellular events, including the tyrosine phosphorylation of a 145-kDa host protein; the reorganization of the host cell actin and associated cellular proteins, like vasodilator-stimulated phosphoprotein, adjacent to the attached bacterial cell; and the subsequent release of the cytokine, interleukin 8 (IL-8). H. pylori isolated from patients with ulcer disease and gastric cancer contain a DNA insertion, the cag pathogenicity island (PAI), that is not present in bacteria isolated from individuals with asymptomatic infection. Mutations in a number of PAI genes abolish tyrosine phosphorylation and IL-8 synthesis but not the cytoskeletal rearrangements. Kinase inhibition studies suggest there are two distinct pathways operative in stimulating IL-8 release from host cells and one of these H. pylori pathways is independent of the tyrosine phosphorylation step.

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“…A full-length murine VASP cDNA was sequenced (see "Ma- terials and Methods"), and the murine VASP protein predicted by the ORF was 87% identical to the human VASP protein (56). All three human VASP cyclic nucleotide-dependent phosphorylation sites are conserved in murine VASP (46).…”

Section: Effect Of Cgki␤ Overexpression On Cre-dependent Genementioning

confidence: 99%

Cyclic AMP- and Cyclic GMP-dependent Protein Kinases Differ in Their Regulation of Cyclic AMP Response Element-dependent Gene Transcription

Collins

Uhler

1999

Journal of Biological Chemistry

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The ability of cGMP-dependent protein kinases (cGKs) to activate cAMP response element (CRE)-dependent gene transcription was compared with that of cAMP-dependent protein kinases (cAKs). Although both the type I␤ cGMP-dependent protein kinase (cGKI␤) and the type II cAMP-dependent protein kinase (cAKII) phosphorylated the cytoplasmic substrate VASP (vasodilator-and A kinase-stimulated phosphoprotein) to a similar extent, cyclic nucleotide regulation of CRE-dependent transcription was at least 10-fold higher in cAKII-transfected cells than in cGKI␤-transfected cells. Overexpression of each kinase in mammalian cells resulted in a cytoplasmic localization of the unactivated enzyme. As reported previously, the catalytic (C) subunit of cAKII translocated to the nucleus following activation by 8-bromo-cyclic AMP. However, cGKI␤ did not translocate to the nucleus upon activation by 8-bromocyclic GMP. Replacement of an autophosphorylated serine (Ser 79 ) of cGKI␤ with an aspartic acid resulted in a mutant kinase with constitutive kinase activity in vitro and in vivo. The cGKI␤S79D mutant localized to the cytoplasm and was only a weak activator of CRE-dependent gene transcription. However, an amino-terminal deletion mutant of cGKI␤ was found in the nucleus as well as the cytoplasm and was a strong activator of CRE-dependent gene transcription. These data suggest that the inability of cGKs to translocate to the nucleus is responsible for the differential ability of cAKs and cGKs to activate CRE-dependent gene transcription and that nuclear redistribution of cGKs is not required for NO/ cGMP regulation of gene transcription.The cyclic nucleotides, cAMP and cGMP, are intracellular second messengers mediating the actions of a large number of hormones and neurotransmitters. These cyclic nucleotides act to allosterically regulate the action of a small number of important proteins. Unlike cAMP, which acts mainly through cAMP-dependent protein kinases (cAKs), 1 cGMP is able to activate three classes of proteins: ion channels, phosphodiesterases, and cGMP-dependent protein kinases (cGKs). The cAKs and the cGKs are highly homologous protein kinase families with similar substrate specificities. Phosphorylation of cellular proteins by both families of kinases leads to alterations in calcium mobilization, protein phosphatase activity, ion channel function, gene transcription, smooth muscle contractility, and platelet aggregation (1-4). The cGKs are classified into two types based on their historical order of characterization. The type I enzymes (cGKIs) are highly expressed in lung (5

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Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP.

Cited by 198 publications

References 45 publications

Homer/Vesl Proteins and Their Roles in CNS Neurons

Homer/Vesl Proteins and Their Roles in CNS Neurons

Induction of host signal transduction pathways by Helicobacter pylori

Cyclic AMP- and Cyclic GMP-dependent Protein Kinases Differ in Their Regulation of Cyclic AMP Response Element-dependent Gene Transcription

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