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Integrin-linked kinase-associated serine/threonine phosphatase

ILKAP, integrin-linked kinase-associated protein phosphatase 2C isoform
The protein encoded by this gene is a protein serine/threonine phosphatase of the PP2C family. This protein can interact with integrin-linked kinase (ILK/ILK1), a regulator of integrin mediated signaling, and regulate the kinase activity of ILK. Through the interaction with ILK, this protein may selectively affect the signaling process of ILK-mediated glycogen synthase kinase 3 beta (GSK3beta), and thus participate in Wnt signaling pathway. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, integrin-linked kinase, AML1, PCNA, POLYMERASE
Papers on ILKAP
ILKAP, ILK and PINCH1 control cell survival of p53-wildtype glioblastoma cells after irradiation.
Eke et al., Dresden, Germany. In Oncotarget, Nov 2015
As the underlying molecular mechanisms remain largely elusive, we addressed whether targeting of the focal adhesion proteins particularly interesting new cysteine-histidine-rich 1 (PINCH1), integrin-linked kinase (ILK) and ILK associated phosphatase (ILKAP) modulates GBM cell radioresistance.
Endometrial ILKAP expression among patients with endometriosis and its association with clinical characteristics.
Liu et al., Jinan, China. In Int J Gynaecol Obstet, Jul 2015
OBJECTIVE: To investigate expression of ILKAP among women with endometriosis and its association with clinical characteristics.
Involvement of ANXA5 and ILKAP in susceptibility to malignant melanoma.
Boyano et al., Leioa, Spain. In Plos One, 2013
Additionally, a second SNP (rs6431588) located on ILKAP was found to be associated with melanoma after considering a combined set of 1,883 MM cases and 1,358 disease-free controls.
Characterization of nuclear localization signal in the N terminus of integrin-linked kinase-associated phosphatase (ILKAP) and its essential role in the down-regulation of RSK2 protein signaling.
Xiao et al., Shanghai, China. In J Biol Chem, 2013
Integrin-linked kinase-associated phosphatase (ILKAP) is a serine/threonine (S/T) phosphatase that belongs to the protein phosphatase 2C (PP2C) family.
Probing protein phosphatase substrate binding: affinity pull-down of ILKAP phosphatase 2C with phosphopeptides.
Gammeltoft et al., Glostrup, Denmark. In Mol Biosyst, 2012
Here we report the application of solid-phase synthesis of phosphopeptides for pull-down and analysis of the affinity profile of the integrin-linked kinase associated phosphatase (ILKAP), a member of the protein phosphatase 2C (PP2C) family.
Genome-wide association study identifies novel loci associated with circulating phospho- and sphingolipid concentrations.
EUROSPAN consortium et al., Rotterdam, Netherlands. In Plos Genet, 2011
Among those, 14 loci (KCNH7, AGPAT1, PNLIPRP2, SYT9, FADS1-2-3, DLG2, APOA1, ELOVL2, CDK17, LIPC, PDXDC1, PLD2, LASS4, and APOE) mapped into the glycerophospholipid and 12 loci (ILKAP, ITGA9, AGPAT1, FADS1-2-3, APOA1, PCDH20, LIPC, PDXDC1, SGPP1, APOE, LASS4, and PLD2) to the sphingolipid pathways.
The LO-BaFL method and ALS microarray expression analysis.
Weller et al., Charlotte, United States. In Bmc Bioinformatics, 2011
High-quality RNA from six healthy Control and six sALS samples yielded the predicted differential expression for 7 genes: TARDBP, SKIV2L2, C12orf35, DYNLT1, ACTG1, B2M, and ILKAP.
Palladin is a novel binding partner of ILKAP in eukaryotic cells.
Zhang et al., Changchun, China. In Biochem Biophys Res Commun, 2011
these results suggested that palladin played a specific role in modulating the subcellular localization of the cytoplasmic ILKAP and promoting the ILKAP-induced apoptosis.
Tumor-specific mutation and downregulation of ING5 detected in oral squamous cell carcinoma.
Nagatsuka et al., Okayama, Japan. In Int J Cancer, 2010
This location contains several candidate tumor suppressor genes such as PPP1R7, ILKAP, DTYMK and ING5.
Modulation of integrin-linked kinase nucleo-cytoplasmic shuttling by ILKAP and CRM1.
Dagnino et al., London, Canada. In Cell Cycle, 2008
These studies demonstrate the importance for keratinocyte proliferation of ILK regulation through changes in its subcellular localization, and establish ILKAP and CRM1 as pivotal modulators of ILK subcellular distribution and activity in these cells.
Role of type 2C protein phosphatases in growth regulation and in cellular stress signaling.
Lavi et al., Heidelberg, Germany. In Crit Rev Biochem Mol Biol, 2007
Here, we provide an overview of the involvement of type 2C phosphatases in these two processes, and we show that four of them (PP2Calpha, PP2Cbeta, ILKAP, and PHLPP) can be expected to function as tumor suppressor proteins, and one as an oncoprotein (PP2Cdelta /Wip1).
Fine deletion mapping of chromosome 2q21-37 shows three preferentially deleted regions in oral cancer.
Nagai et al., Okayama, Japan. In Oral Oncol, 2007
Several candidate tumor suppressor genes in these regions such as LRP1B, CASP8, CASP10, BARD1, ILKAP, PPP1R7, and ING5, are located.
PP2C family members play key roles in regulation of cell survival and apoptosis.
Kobayashi et al., Sendai, Japan. In Cancer Sci, 2006
In contrast, PP2Cdelta/ILKAP, a second PP2C family member, activates ASK1 by enhancing cellular phosphorylation of T845.
Proteomic analysis of differentially expressed proteins between metastatic and non-metastatic human colorectal carcinoma cell lines.
Yi-Li et al., Xi'an, China. In Eur J Gastroenterol Hepatol, 2005
RESULTS: The protein endothelial cell growth factor 1 (platelet-derived), rhotekin protein (RTKN), septin 1, cyclin-dependent kinase 1, sialic acid binding Ig-like lectin 11, tyrosinase-related protein-2, translin-like protein, and DNA directed RNA polymerase II polypeptide J-related gene isoform 2 appeared in metastatic but were not detected in non-metastatic cell lines, whereas integrin-linked kinase-associated protein phosphatase 2C isoform 2, MHC class I promoter binding protein, protein phosphatase 2A regulatory subunit B' (PR 53), carboxypeptidase A5, paired box transcription factor, zinc finger protein 79, and apolipoprotein B-48 were detected in non-metastatic but were absent in metastatic cell lines.
ILKAP regulates ILK signaling and inhibits anchorage-independent growth.
Hannigan et al., Toronto, Canada. In Oncogene, 2004
ILKAP is a protein phosphatase 2C that selectively associates with integrin linked kinase, ILK, to modulate cell adhesion and growth factor signaling.
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