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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 24 Oct 2014.

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
An improved recombinant Fab-immunotoxin targeting CD22 expressing malignancies.
New
Pastan et al., Bethesda, United States. In Leuk Res, 31 Oct 2014
Moxetumomab pasudotox (HA22) is a recombinant immunotoxin, now in clinical trials, that combines an anti-CD22-Fv with a 38-kDa fragment of Pseudomonas exotoxin A. To produce a less immunogenic molecule without reducing the half-life in circulation, we constructed LMB11 combining an anti-CD22 Fab with a less immunogenic version of PE38.
Role of the ANKMY2-FKBP38 Axis in Regulation of the Sonic Hedgehog (Shh) Signaling Pathway.
New
Nakayama et al., Fukuoka, Japan. In J Biol Chem, 12 Oct 2014
Ablation of the FK506-binding protein 38 (FKBP38) gene results in activation of the Shh signaling pathway in mouse embryos, but the molecular mechanism by which FKBP38 suppresses Shh signaling has remained unclear.
Aminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella, participates in parasite development.
New
Brossier et al., Tours, France. In Eukaryot Cell, Jul 2014
EtAPN1 is synthesized as a 120-kDa precursor and cleaved into 96-, 68-, and 38-kDa forms during sporulation.
Cytoadherence phenotype of Plasmodium falciparum-infected erythrocytes is associated with specific pfemp-1 expression in parasites from children with cerebral malaria.
New
Tahar et al., Paris, France. In Malar J, Dec 2013
This biological process is thought to be mediated by P. falciparum erythrocyte membrane protein-1 (PfEMP-1) and human receptors such as CD36 and ICAM-1.
Establishment of a quantitative PCR system for discriminating chitinase-like proteins: catalytically inactive breast regression protein-39 and Ym1 are constitutive genes in mouse lung.
New
Oyama et al., Hachiōji, Japan. In Bmc Mol Biol, Dec 2013
Mice express primarily three CLPs, including breast regression protein-39 (BRP-39) [chitinase 3-like-1 (Chi3l1) or 38-kDa glycoprotein (gp38k)], Ym1 (Chi3l3) and Ym2 (Chi3l4).
Role of Bcl-2 in tumour cell survival and implications for pharmacotherapy.
Review
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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+).
Molecular Characterization and Tissue-specific Expression of a Novel FKBP38 Gene in the Cashmere Goat (Capra hircus).
Liu et al., Hohhot, China. In Asian-australas J Anim Sci, 2012
As a member of a subclass of immunophilins, it is controversial that FKBP38 acts an upstream regulator of mTOR signaling pathway, which control the process of cell-growth, proliferation and differentiation.
FKBP38 peptidylprolyl isomerase promotes the folding of cystic fibrosis transmembrane conductance regulator in the endoplasmic reticulum.
GeneRIF
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.
Review
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.
Review
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.
Review
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.
GeneRIF
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.
Detection of Antibodies Against 6, 16 and 38 kDa Antigens of Mycobacterium tuberculosis as a Rapid Test for Diagnosis of Tuberculosis.
Velayati et al., Tehrān, Iran. In Tanaffos, 2010
MATERIALS AND METHODS: The tuberculosis rapid test device based on detection of IgM, IgA and IgG antibodies against 6, 16 and 38-kDa antigens of Mycobacterium tuberculosis via chromatography was used in 96 cases of pulmonary and extra pulmonary TB.
FK506 binding proteins as targets in anticancer therapy.
Review
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.
Impact
GeneRIF
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.
Impact
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.
Impact
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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