scholarly journals Mutations in a Gene Encoding a Novel Protein Containing a Phosphotyrosine-Binding Domain Cause Type 2 Cerebral Cavernous Malformations

2003 ◽  
Vol 73 (6) ◽  
pp. 1459-1464 ◽  
Author(s):  
Christina L. Liquori ◽  
Michel J. Berg ◽  
Adrian M. Siegel ◽  
Elizabeth Huang ◽  
Jon S. Zawistowski ◽  
...  
Keyword(s):  
Binding Domain ◽  
Cerebral Cavernous Malformations ◽  
Gene Encoding ◽  
Cavernous Malformations ◽  
Phosphotyrosine Binding Domain ◽  
Novel Protein

Germline mutations in theCCM1 gene, encoding Krit1, cause cerebral cavernous malformations

2001 ◽  
Vol 49 (4) ◽  
pp. 529-532 ◽  
Author(s):  
Miguel Lucas ◽  
Alzenira F. Costa ◽  
Mariano Montori ◽  
Francisca Solano ◽  
Mar�a D. Zayas ◽  
...  
Keyword(s):  
Germline Mutations ◽  
Cerebral Cavernous Malformations ◽  
Gene Encoding ◽  
Cavernous Malformations

scholarly journals Role for Vitamin B12 in Light Induction of Gene Expression in the Bacterium Myxococcus xanthus

2002 ◽  
Vol 184 (8) ◽  
pp. 2215-2224 ◽  
Author(s):  
María Cervantes ◽  
Francisco J. Murillo
Keyword(s):  
Myxococcus Xanthus ◽  
Carotenoid Biosynthesis ◽  
Inducible Promoter ◽  
Binding Domain ◽  
Gene Encoding ◽  
The Family ◽  
Mutant Strains ◽  
Carotenoid Genes ◽  
Carotenoid Synthesis ◽  
Novel Protein

ABSTRACT A light-inducible promoter (PB) drives the carB operon (carotenoid genes) of the bacterium Myxococcus xanthus. A gene encoding a regulator of carotenoid biosynthesis was identified by studying mutant strains carrying a transcriptional fusion to PB and deletions in three candidate genes. Our results prove that the identified gene, named carA, codes for a repressor of the PB promoter in the dark. They also show that the carA gene product does not participate in the light activation of two other promoters connected with carotenoid synthesis or its regulation in M. xanthus. CarA is a novel protein consisting of a DNA-binding domain of the family of MerR helix-turn-helix transcriptional regulators, directly joined to a cobalamin-binding domain. In support of this, we report here that the presence of vitamin B12 or some other cobalamin derivatives is absolutely required for activation of the PB promoter by light.

scholarly journals Mutations in the Gene Encoding KRIT1, a Krev-1/rap1a Binding Protein, Cause Cerebral Cavernous Malformations (CCM1)

1999 ◽  
Vol 8 (12) ◽  
pp. 2325-2333 ◽  
Author(s):  
T. Sahoo ◽  
E. W. Johnson ◽  
J. W. Thomas ◽  
P. M. Kuehl ◽  
T. L. Jones ◽  
...  
Keyword(s):  
Binding Protein ◽  
Cerebral Cavernous Malformations ◽  
Gene Encoding ◽  
Cavernous Malformations

scholarly journals A Series of 14 Representative Presentations of Cerebral Cavernous Malformations

2021 ◽  
pp. 101298
Author(s):  
Ryan Hudnall ◽  
Eric X. Chen ◽  
Patrick J Opperman ◽  
Sean Kelly ◽  
Justin A. Cramer ◽  
...  
Keyword(s):  
Cerebral Cavernous Malformations ◽  
Cavernous Malformations

scholarly journals Missense mutations in theTGM2 gene encoding transglutaminase 2 are found in patients with early-onset type 2 diabetes

2007 ◽  
Vol 28 (11) ◽  
pp. 1150-1150 ◽  
Author(s):  
O. Porzio ◽  
O. Massa ◽  
V. Cunsolo ◽  
C. Colombo ◽  
M. Malaponti ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Early Onset ◽  
Transglutaminase 2 ◽  
Missense Mutations ◽  
Gene Encoding ◽  
Onset Type

Genotype-phenotype correlations in cerebral cavernous malformations patients

2006 ◽  
Vol 60 (5) ◽  
pp. 550-556 ◽  
Author(s):  
Christian Denier ◽  
Pierre Labauge ◽  
Françoise Bergametti ◽  
Florence Marchelli ◽  
Florence Riant ◽  
...  
Keyword(s):  
Cerebral Cavernous Malformations ◽  
Cavernous Malformations

scholarly journals Serine Phosphorylation Proximal to Its Phosphotyrosine Binding Domain Inhibits Insulin Receptor Substrate 1 Function and Promotes Insulin Resistance

2004 ◽  
Vol 24 (21) ◽  
pp. 9668-9681 ◽  
Author(s):  
Yan-Fang Liu ◽  
Avia Herschkovitz ◽  
Sigalit Boura-Halfon ◽  
Denise Ronen ◽  
Keren Paz ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Insulin Receptor ◽  
Insulin Signaling ◽  
Insulin Treatment ◽  
Binding Domain ◽  
Serine Phosphorylation ◽  
Insulin Receptor Substrate ◽  
Control Mechanisms ◽  
Insulin Receptor Substrate 1 ◽  
Phosphotyrosine Binding Domain

ABSTRACT Ser/Thr phosphorylation of insulin receptor substrate (IRS) proteins negatively modulates insulin signaling. Therefore, the identification of serine sites whose phosphorylation inhibit IRS protein functions is of physiological importance. Here we mutated seven Ser sites located proximal to the phosphotyrosine binding domain of insulin receptor substrate 1 (IRS-1) (S265, S302, S325, S336, S358, S407, and S408) into Ala. When overexpressed in rat hepatoma Fao or CHO cells, the mutated IRS-1 protein in which the seven Ser sites were mutated to Ala (IRS-17A), unlike wild-type IRS-1 (IRS-1WT), maintained its Tyr-phosphorylated active conformation after prolonged insulin treatment or when the cells were challenged with inducers of insulin resistance prior to acute insulin treatment. This was due to the ability of IRS-17A to remain complexed with the insulin receptor (IR), unlike IRS-1WT, which underwent Ser phosphorylation, resulting in its dissociation from IR. Studies of truncated forms of IRS-1 revealed that the region between amino acids 365 to 430 is a main insulin-stimulated Ser phosphorylation domain. Indeed, IRS-1 mutated only at S408, which undergoes phosphorylation in vivo, partially maintained the properties of IRS-17A and conferred protection against selected inducers of insulin resistance. These findings suggest that S408 and additional Ser sites among the seven mutated Ser sites are targets for IRS-1 kinases that play a key negative regulatory role in IRS-1 function and insulin action. These sites presumably serve as points of convergence, where physiological feedback control mechanisms, which are triggered by insulin-stimulated IRS kinases, overlap with IRS kinases triggered by inducers of insulin resistance to terminate insulin signaling.

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