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Results suggest that loss of PRKCSH and SEC63 leads to general defects in ciliogenesis, while quenching of the Wnt signaling cascade is cholangiocyte-restricted.
This study demonstrated that Large copy number variations on germline level are not present in patients with a clinical diagnosis of Severe Polycystic Liver Disease.
Polycystic liver disease is recessive at the cellular level, and loss of functional PRKCSH is an important step in cystogenesis.
The induction of autophagy by hepatocystin deficiency is mediated through mammalian target of rapamycin (mTOR).
Results provide evidence that mutations at the coding PRKCSH GAG repeat are a target of MSI and are selectively associated with the MSI-H phenotype in gastric carcinomas.
The common SNPs tested in DDOST, PRKCSH and LGALS3 do not seem to be associated with diabetic micro- or macrovascular complications or with type 1 diabetes in Finnish patients.
identified a total of 26 novel mutations in PRKCSH (n = 14) and SEC63 (n = 12), including four splice site mutations, eight insertions/ deletions, six non-sense mutations, and eight missense mutations
Our results suggest that PRKCSH gene is not a major genetic cause of PCLD and there may be at least another locus responsible for the disease in Taiwan.
PRKCSH functions as a chaperone-like molecule, which prevents endoplasmic reticulum-associated degradation of TRPP2.
Mutations in this protein cause isolated autosomal dominant polycystic liver disease.
germline mutations in PRKCSH as the probable cause of autosomal dominant polycystic liver disease
autosomal dominant polycystic liver disease is genetically heterogeneous
role of hepatocystin in carbohydrate processing and quality control of newly synthesized glycoproteins in the endoplasmic reticulum
results identify 80K-H as a new player involved in GLUT4 vesicle transport and identify a link between a kinase involved in the insulin signalling cascade, PKCzeta, and a known component of the GLUT4 vesicle trafficking pathway, munc18c
the majority of cysts from PRKCSH mutation carriers did not express hepatocystin
Hepatocystin is not secreted in liver cyst fluids of autosomal dominant polycystic liver disease patients, suggesting that mutant hepatocystin is either not produced or degraded intracellularly.
80K-H is a novel regulator of IP3R1 activity, and it may contribute to neuronal functions.
These results indicate that insulin induces dynamic associations between PKCzeta, 80K-H, and munc18c and that 80K-H may act as a key signaling link between PKCzeta and munc18c in live cells.
TRIM67 regulates Ras signaling via degradation of 80K-H, leading to neural differentiation including neuritogenesis.
Data demonstrate the presence of a binding site on the 3'-untranslated region of NR1 mRNA for AnxA2 and show the regulation of NR1 mRNA by AnxA2, GIIbeta and a third NR1 mRNA-binding protein, which is yet to be identified.
80K-H is a Ca(2+) sensor controlling TRPV5 channel activity
This study is the first to report that VASAP-60 is up-regulated in granulosa cells of dominant follicles, to document the primary structure of the VASAP-60 gene and the YY1 binding to promoter may act as a positive transcriptional regulator.
This gene encodes the beta-subunit of glucosidase II, an N-linked glycan-processing enzyme in the endoplasmic reticulum (ER). This protein is an acidic phospho-protein known to be a substrate for protein kinase C. Mutations in this gene have been associated with the autosomal dominant polycystic liver disease (PCLD). Alternatively spliced transcript variants encoding distinct isoforms have been observed.
AGE-binding receptor 2
, glucosidase 2 subunit beta
, glucosidase II subunit beta
, glucosidase II, beta subunit
, protein kinase C substrate 60.1 kDa protein heavy chain
, protein kinase C substrate, 80 Kda protein
, alpha glucosidase II, beta-subunit
, carbohydrate processing enzyme of the endoplasmic reticulum
, glucosidase II beta-subunit
, 80K-H protein
, vacuolar system associated protein-60
, vacuolar system-associated protein 60
, protein kinase C substrate 80K-H
, phospholipase D1, phosphatidylcholine-specific