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None of the Polymorphous low-grade adenocarcinoma (PLGA) lacking PRKD1 (show PRKD1 Proteins) somatic mutations or PRKD gene family rearrangements harboured somatic mutations in the kinase domains of the PRKD2 or PRKD3 (show PRKD3 Proteins) genes.
investigated the interaction network of human PKD2 in the cytosol and in Golgi-enriched subcellular protein fractions
SNX3 (show SNX3 Proteins)-retromer complex regulates the surface expression and function of PC1 (show PCSK1 Proteins) and PC2 (show KRT6B Proteins)
We aimed to revisit PKD2 prevalence, clinical presentation, mutation spectrum, and prognosis through the Genkyst cohort. Patients with PKD2-related dominant polycystic kidney disease typically present with mild disease
Hyperactivation of the ERK (show EPHB2 Proteins) pathway may be caused by down-regulation of PC-1 (show PCSK1 Proteins) and PC-2 (show KRT6B Proteins) in lymphatic malformations, contributing to increased proliferation of lymphatic endothelial cells.
Annualized median liver growth rates were 1.68, 1.5 and 1.24% for PKD1 (show PKD1 Proteins)-T, PKD1 (show PKD1 Proteins)-NT and PKD2 mutations, respectively (P = 0.49), and remained unaffected by the ADPKD genotype when adjusted for age, gender and baseline HtLV.
Here, we review previous studies that connect the molecular properties of the domains of PC2 (show KRT6B Proteins) Cterm to distinct aspects of PC2 (show KRT6B Proteins) functions and regulation.
Data show that in 82 (87.2%) of the patients, pathogenic mutations were detected in PKD1 (show PKD1 Proteins) (79.0%-92.5%), whereas in 12 (12.8%) patients pathogenic mutations were detected in PKD2 (7.5%-21.0%).
Two cryo-EM structures of distinct channel states of full-length human PC2 (show KRT6B Proteins) in complex with lipids and cations.
The structure of human PC2 (show KRT6B Proteins) in a closed conformation, solved by electron cryomicroscopy at 4.2-A resolution.
Our studies demonstrate that PKD1 (show PKD1 Proteins)/2 is a key regulator of MVB maturation and exosome secretion, and constitutes a mediator of the DGK alpha (show DGKA Proteins) effect on MVB secretory traffic.
Results reveal that whereas protein kinase D1 (show PRKD1 Proteins) and protein kinase D2 are essential for neuronal polarity, there exists a functional redundancy between the two proteins.
PKD2 acted as an amplification checkpoint for antigen-stimulated digital cytokine responses and translated the differential strength of TCR signaling to determine the number of naive CD8 (show CD8A Proteins)(+) T cells that became effector cells.
Protein kinase D2 promotes in vitro osteoclast differentiation and fusion
A bioinformatic screen identified the serine-threonine kinase (show CDK4 Proteins) protein kinase D2 (PRKD2) as a potential effector of GABP in hematopoietic stem cells
Transcriptional profiling reveals the full consequences of PKD2 loss and maps in detail the selective, but critical, function for PKD2 in signalling by alpha/beta mature TCR complexes in peripheral T-cells.
PKD2 is a common signaling target downstream of various agonist receptors in platelets and G(q)-mediated signals along with calcium and novel PKC isoforms, in particular, PKCdelta (show PKCd Proteins) activate PKD2 in platelets.
Data demonstrate that, unlike PKD1 (show PKD1 Proteins), PKD2 catalytic activity is dispensable for normal embryogenesis.
PKD2, like PKD (show PRKD1 Proteins), facilitates mitogenesis in 3T3 cells
The protein encoded by this gene belongs to the protein kinase D (PKD) family of serine/threonine protein kinases. This kinase can be activated by phorbol esters as well as by gastrin via the cholecystokinin B receptor (CCKBR) in gastric cancer cells. It can bind to diacylglycerol (DAG) in the trans-Golgi network (TGN) and may regulate basolateral membrane protein exit from TGN. Alternative splicing results in multiple transcript variants encoding different isoforms.
protein kinase D2
, serine/threonine-protein kinase D2-like
, autosomal dominant polycystic kidney disease type II protein
, transient receptor potential cation channel, subfamily P, member 2
, serine/threonine-protein kinase D2