Identification and Characterization of a New Human Gene Encoding a Small Protein with High Homology to the Proline-Rich Region of the SH3BGR Gene

1998 ◽  
Vol 247 (2) ◽  
pp. 302-306 ◽  
Author(s):  
Aliana Egeo ◽  
Michela Mazzocco ◽  
Patrizio Arrigo ◽  
José M. Vidal-Taboada ◽  
Rafael Oliva ◽  
...  
Keyword(s):  
Human Gene ◽  
High Homology ◽  
Rich Region ◽  
Gene Encoding ◽  
Small Protein ◽  
Identification And Characterization ◽  
Proline Rich Region

scholarly journals Identification and Characterization of the Murine and Human Gene Encoding the Tuberoinfundibular Peptide of 39 Residues

Endocrinology ◽  
2002 ◽  
Vol 143 (3) ◽  
pp. 1047-1057 ◽  
Author(s):  
Markus R. John ◽  
Maya Arai ◽  
David A. Rubin ◽  
Kenneth B. Jonsson ◽  
Harald Jüppner
Keyword(s):  
Human Gene ◽  
Gene Encoding ◽  
Tuberoinfundibular Peptide ◽  
Identification And Characterization

scholarly journals Identification and Characterization of Novel Mutations in the Human Gene Encoding the Catalytic Subunit Calpha of Protein Kinase A (PKA)

PLoS ONE ◽  
2012 ◽  
Vol 7 (4) ◽  
pp. e34838 ◽  
Author(s):  
Kristoffer Søberg ◽  
Anja C. V. Larsen ◽  
Mandy Diskar ◽  
Paul H. Backe ◽  
Magnar Bjørås ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Human Gene ◽  
Catalytic Subunit ◽  
Novel Mutations ◽  
Gene Encoding ◽  
Identification And Characterization ◽  
Kinase A

scholarly journals Contribution of Ena/VASP Proteins to Intracellular Motility ofListeriaRequires Phosphorylation and Proline-rich Core but Not F-Actin Binding or Multimerization

2002 ◽  
Vol 13 (7) ◽  
pp. 2383-2396 ◽  
Author(s):  
Marcus Geese ◽  
Joseph J. Loureiro ◽  
James E. Bear ◽  
Jürgen Wehland ◽  
Frank B. Gertler ◽  
...  
Keyword(s):  
Bacterial Motility ◽  
Actin Binding ◽  
Rich Region ◽  
Bacterial Surface ◽  
Identification And Characterization ◽  
Actin Binding Site ◽  
Intracellular Motility ◽  
Proline Rich Region

The Listeria model system has been essential for the identification and characterization of key regulators of the actin cytoskeleton such as the Arp2/3 complex and Ena/vasodilator-stimulated phosphoprotein (VASP) proteins. Although the role of Ena/VASP proteins in Listeria motility has been extensively studied, little is known about the contributions of their domains and phosphorylation state to bacterial motility. To address these issues, we have generated a panel of Ena/VASP mutants and, upon expression in Ena/VASP-deficient cells, evaluated their contribution to Ena/VASP function in Listeria motility. The proline-rich region, the putative G-actin binding site, and the Ser/Thr phosphorylation of Ena/VASP proteins are all required for efficientListeria motility. Surprisingly, the interaction of Ena/VASP proteins with F-actin and their potential ability to form multimers are both dispensable for their involvement in this process. Our data suggest that Ena/VASP proteins contribute toListeria motility by regulating both the nucleation and elongation of actin filaments at the bacterial surface.

Chromosomal localization and preliminary characterization of the human gene encoding insulin-like growth factor II

1985 ◽  
Vol 69 (2) ◽  
pp. 170-173 ◽  
Author(s):  
P. de Pagter-Holthuizen ◽  
J. W. M. Höppener ◽  
M. Jansen ◽  
A. H. M. Geurts van Kessel ◽  
G. J. B. van Ommen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Chromosomal Localization ◽  
Human Gene ◽  
Insulin Like Growth Factor ◽  
Gene Encoding ◽  
Preliminary Characterization ◽  
Factor Ii

scholarly journals Identification and characterization of YLR328W, theSaccharomyces cerevisiaestructural gene encoding NMN adenylyltransferase. Expression and characterization of the recombinant enzyme

FEBS Letters ◽  
1999 ◽  
Vol 455 (1-2) ◽  
pp. 13-17 ◽  
Author(s):  
Monica Emanuelli ◽  
Francesco Carnevali ◽  
Maria Lorenzi ◽  
Nadia Raffaelli ◽  
Adolfo Amici ◽  
...  
Keyword(s):  
Recombinant Enzyme ◽  
Gene Encoding ◽  
Identification And Characterization

Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p

1998 ◽  
Vol 111 (10) ◽  
pp. 1341-1349 ◽  
Author(s):  
M. Imoto ◽  
I. Tachibana ◽  
R. Urrutia
Keyword(s):  
Endoplasmic Reticulum ◽  
Cho Cells ◽  
Mammalian Cells ◽  
Functional Characterization ◽  
Luciferase Reporter ◽  
Pleckstrin Homology ◽  
Rich Region ◽  
Gtpase Domain ◽  
Proline Rich Region

Dynamin proteins containing a GTPase domain, a pleckstrin homology motif and a proline-rich tail participate in receptor-mediated endocytosis in organisms ranging from insects to vertebrates. In addition, dynamin-related GTPases, such as the yeast Golgi protein Vps1p, which lack both the pleckstrin homology motif and the proline-rich region, participate in vesicular transport within the secretory pathway in lower eukaryotes. However, no data is available on the existence of Vps1p-like proteins in mammalian cells. In this study, we report the identification and characterization of a novel gene encoding a human dynamin-related protein, DRP1, displaying high similarity to the Golgi dynamin-like protein Vps1p from yeast and to a Caenorhabditis elegans protein deposited in the databank. These proteins are highly conserved in their N-terminal tripartite GTPase domain but lack the pleckstrin homology motif and proline-rich region. Northern blot analysis reveals that the DRP1 mRNA is detected at high levels in human muscle, heart, kidney and brain. Immunolocalization studies in Chinese hamster ovary (CHO) cells using an epitope-tagged form of DRP1 and confocal microscopy show that this protein is concentrated in a perinuclear region that labels with the endoplasmic reticulum marker DiOC6(3) and the Golgi marker C5-DMB-Cer. In addition, the localization of DRP1 is highly similar to the localization of the endoplasmic reticulum and cis-Golgi GTPase Rab1A, but not to the staining for the trans-Golgi GTPase Rab6. Furthermore, overexpression of a cDNA encoding a GTP binding site mutant of DRP1 (DRP1(K38E)) in CHO cells decreases the amount of a secreted luciferase reporter protein, whereas the overexpression of wild-type DRP1 increases the secretion of this marker. Together, these results constitute the first structural and functional characterization of a mammalian protein similar to the yeast dynamin-related GTPase Vps1p and indicate that the participation of these proteins in secretion has been conserved throughout evolution.

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