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Membrane protein, palmitoylated 1, 55kDa

38-kDa, MPPI, erythrocyte membrane protein-1, FKBP38
This gene encodes the prototype of the membrane-associated guanylate kinase (MAGUK) family proteins. MAGUKs interact with the cytoskeleton and regulate cell proliferation, signaling pathways, and intercellular junctions. The encoded protein is an extensively palmitoylated membrane phosphoprotein containing a PDZ domain, a Src homology 3 (SH3) motif, and a guanylate kinase domain. This gene product interacts with various cytoskeletal proteins and cell junctional proteins in different tissue and cell types, and may be involved in the regulation of cell shape, hair cell development, neural patterning of the retina, and apico-basal polarity and tumor suppression pathways in non-erythroid cells. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, fibrillin-1, V1a
Papers on 38-kDa
A Survey of the Interactome of Kaposi's Sarcoma-Associated Herpesvirus ORF45 Revealed Its Binding to Viral ORF33 and Cellular USP7, Resulting in Stabilization of ORF33 That Is Required for Production of Progeny Viruses.
Zhu et al., Tallahassee, United States. In J Virol, 01 Jun 2015
Mass spectrometry revealed that the 38-kDa protein is viral ORF33 and the 130-kDa protein is cellular USP7 (ubiquitin-specific protease 7).
Mycobacterium tuberculosis 38-kDa antigen induces endoplasmic reticulum stress-mediated apoptosis via toll-like receptor 2/4.
Song et al., Taejŏn, South Korea. In Apoptosis, 31 Mar 2015
To investigate the regulatory role of the ER stress response in 38-kDa antigen-induced apoptosis, we examined the relationship between the ER stress response and apoptosis in bone marrow-derived macrophages (BMDMs) stimulated with Mycobacterium tuberculosis antigen (38-kDa Ag).
Evaluation of antigen-specific immunoglobulin g responses in pulmonary tuberculosis patients and contacts.
Cho et al., Seoul, South Korea. In J Clin Microbiol, 31 Mar 2015
Serum IgG responses to selective M. tuberculosis antigens, including the 38-kDa and 16-kDa antigens, lipoarabinomannan (LAM), and recombinant early secreted antigen target 6 kDa (ESAT-6) and culture filtrate protein 10 kDa (CFP-10), were determined.
A novel immunotoxin - rCCK8PE38 targeting of CCK-R overexpressed colon cancers.
Liu et al., Changchun, China. In J Drug Target, 12 Mar 2015
Methods: To construct the CCKR-targeted IT, a reverse CCK8 peptide was fused with a modified 38-kDa truncated form of the Pseudomonas exotoxin (PE38KDEL).
PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an adhesin, which binds the macrophage mannose receptor and promotes phagocytosis.
Mancilla et al., Mexico. In Scand J Immunol, Jan 2015
Among these proteins, we identified PstS-1, a 38-kDa M. tuberculosis mannosylated glycolipoprotein, and characterized it as an adhesin.
Dynamic association of PfEMP1 and KAHRP in knobs mediates cytoadherence during Plasmodium invasion.
Bhavesh et al., Mumbai, India. In Sci Rep, Dec 2014
The knob associated histidine rich protein (KAHRP) is indispensable to knob formation and has been implicated in the recruitment and tethering of P. falciparum erythrocyte membrane protein-1 (PfEMP1) by binding to its cytoplasmic domain termed VARC.
Tetratricopeptide Repeat Domain 9A Negatively Regulates Estrogen Receptor Alpha Activity.
Lin et al., Singapore, Singapore. In Int J Biol Sci, Dec 2014
Although TTC9A does not bind to ERα or its chaperone protein Hsp90 directly, TTC9A strongly interacts with FKBP38 and FKBP51, both of which interact with ERα and Hsp90 and modulate ERα activity.
Role of Bcl-2 in tumour cell survival and implications for pharmacotherapy.
Dass et al., Australia. In J Pharm Pharmacol, 2012
FKBP-38 is a binding protein that has been discovered to be upregulated in highly aggressive cancers and binds to Bcl-2 rather than the pro-apoptotics to induce a state of hyper-mitosis.
FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability.
Balch et al., Los Angeles, United States. In J Biol Chem, 2012
FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability
Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells.
Sikorski et al., Wrocław, Poland. In J Biol Chem, 2012
pathophysiological relationship between the loss of MPP1-directed palmitoylation activity and perturbed lateral membrane organization.
The FKBP38 catalytic domain binds to Bcl-2 via a charge-sensitive loop.
Lücke et al., Halle, Germany. In J Biol Chem, 2012
The derived structure model of the complex between Bcl-2 and the FKBP38 catalytic domain features both electrostatic and hydrophobic intermolecular contacts and provides a rationale for the regulation of the FKBP38/Bcl-2 interaction by Ca(2+).
FKBP38 peptidylprolyl isomerase promotes the folding of cystic fibrosis transmembrane conductance regulator in the endoplasmic reticulum.
Wang et al., Toledo, United States. In J Biol Chem, 2012
Data support a dual role for FKBP38 in regulating CFTR synthesis and post-translational folding.
Antibody fusion proteins: anti-CD22 recombinant immunotoxin moxetumomab pasudotox.
Pastan et al., Bethesda, United States. In Clin Cancer Res, 2011
Moxetumomab pasudotox, previously called HA22 or CAT-8015, is a recombinant immunotoxin composed of the Fv fragment of an anti-CD22 monoclonal antibody fused to a 38-kDa fragment of Pseudomonas exotoxin A, called PE38.
FKBP38-Bcl-2 interaction: a novel link to chemoresistance.
Yoon et al., Singapore, Singapore. In Curr Opin Pharmacol, 2011
FKBP38, a noncanonical member of the immunosuppressive drug FK506 binding protein (FKBP) family members, possesses an inducible rotamase.
From cell death to viral replication: the diverse functions of the membrane-associated FKBP38.
Lücke et al., Bethesda, United States. In Curr Opin Pharmacol, 2011
FKBP38 is in many ways an exceptional member of the FK506-binding proteins.
Temporal expression pattern of Fkbp8 in rodent cochlea.
Blin et al., Tübingen, Germany. In Cell Physiol Biochem, 2010
In pre-hearing time Fkbp8-specific signal was also observed in the tectorial membrane, whose alpha- and beta-Tectorin components show similar time-dependent expression of mRNA as Fkbp8.
FK506 binding proteins as targets in anticancer therapy.
Romano et al., Napoli, Italy. In Anticancer Agents Med Chem, 2010
Recent studies have focused on FKBPs in apoptosis regulation: Targeting of FKBP12 promotes apoptosis in chronic lymphocytic leukemia, FKBP38 knockdown sensitizes hepatoma cells to apoptosis, and FKBP51 silencing overcomes resistance to apoptosis in acute lymphoblastic leukemia, prostate cancer, melanoma, and glioma.
Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38.
Jiang et al., Pittsburgh, United States. In Science, 2007
findings suggest that FKBP38 is an endogenous inhibitor of mTOR, whose inhibitory activity is antagonized by Rheb in response to growth factor stimulation and nutrient availability
Abnormal display of PfEMP-1 on erythrocytes carrying haemoglobin C may protect against malaria.
Wellems et al., Bethesda, United States. In Nature, 2005
falciparum erythrocyte membrane protein-1), correlates with these findings.
Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis.
Nakayama et al., Fukuoka, Japan. In Nat Cell Biol, 2003
Here we show that mitochondrial FK506-binding protein 38 (FKBP38), unlike FKBP12, binds to and inhibits calcineurin in the absence of the immunosuppressant FK506, suggesting that FKBP38 is an inherent inhibitor of this phosphatase.
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