Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P11021 (BiP)
 2,049 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have developed assays using cells and isolated membranes to identify factors mediating fusion of the ER-nuclear membrane network in yeast. When cells containing distinctly tagged ER-nuclear envelope membranes are observed during mating, the markers of both parental membranes become colocalized in a process sharing a genetic requirement with karyogamy. Using isolated membranes, we find that fusion between ER compartments requires ATP, but not cytosol, Sec17p (alpha-SNAP), or Sec18p (NSF), the latter two being required at the fusion step in vesicular transport. Proteins tightly associated with the ER membrane are essential for fusion, as is Kar2p (BiP), an ER lumenal hsp70 homolog. BiP may activate an ER-localized fusogen, allowing nuclear fusion and karyogamy in yeast.
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PMID:The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion. 803 15

Nitric oxide is implicated in modulation of memory and pharmacological as well as genetic inhibition of neuronal nitric oxide synthase (nNOS) leads to impaired cognitive function. We therefore decided to study learning and memory functions and cognitive flexibility in the Morris water maze (MWM) in 1-month-old male mice lacking nNOS (nNOS KO). Hippocampal protein profiling was carried out to possibly link protein derangement to impaired cognitive function. Two-dimensional gel electrophoresis with in-gel digestion of spots and subsequent MALDI-TOF identification of proteins and quantification of proteins using specific software was applied. In the memory as well as in the relearning task of the MWM, most of the nNOS KO failed to find the submerged platform within a given time. Proteomic evaluation of hippocampus, the main anatomical structure computing cognitive functions, revealed aberrant expression of a synaptosomal associated protein of the exocytotic machinery (NSF), glycolytic enzymes, chaperones 78 kDa glucose-regulated protein, T-complex protein 1; the signaling structure guanine nucleotide-binding protein G(I)/G(S)/G(T) and heterogeneous nuclear ribonucleoprotein H of the splicing machinery. We conclude that nNOS knockout mice show impaired spatial performance in the MWM, a finding that may be either linked to direct effects of nNOS/NO and/or to specific hippocampal protein derangements.
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PMID:Impaired cognitive performance in neuronal nitric oxide synthase knockout mice is associated with hippocampal protein derangements. 1560 44