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Transmembrane emp24-like trafficking protein 10

TMP21, Tmp21-I, TMED10
This gene is a member of the EMP24/GP25L/p24 family and encodes a protein with a GOLD domain. This type I membrane protein is localized to the plasma membrane and golgi cisternae and is involved in vesicular protein trafficking. The protein is also a member of a heteromeric secretase complex and regulates the complex's gamma-secretase activity without affecting its epsilon-secretase activity. Mutations in this gene have been associated with early-onset familial Alzheimer's disease. This gene has a pseudogene on chromosome 8. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CYP1A1, Presenilin-1, APP, Nicastrin, CAN
Papers on TMP21
TMP21 modulates cell growth in papillary thyroid cancer cells by inducing autophagy through activation of the AMPK/mTOR pathway.
Liu et al., Shanghai, China. In Int J Clin Exp Pathol, 2014
METHODS: The recombinant expression vector pcDNA3.1 (+)-TMP21 and specific small interfering RNAs (siRNA) against TMP21 were transfected into a papillary thyroid cancer cell line (TPC1).
Rat chondrocyte-associated antigen identified as sialylated transmembrane protein Tmp21 belonging to the p24 protein family.
Moskalewski et al., Warsaw, Poland. In Calcif Tissue Int, 2014
Protein sequence analysis of 23-kDa chondrocyte-associated antigen (CAA) revealed that it corresponds to transmembrane Tmp21 protein belonging to the p24 protein family.
Screening of cellular proteins that interact with the classical swine fever virus non-structural protein 5A by yeast two-hybrid analysis.
Zhang et al., China. In J Biosci, 2014
Alignment with the NCBI database revealed 16 interactive proteins: DDX5, PSMC3, NAV1, PHF5A, GNB2L1, CSDE1, HSPA8, BRMS1, PPP2R3C, AIP, TMED10, POLR1C, TMEM70, METAP2, CHORDC1 and COPS6.
Identification of pre-erythrocytic malaria antigens that target hepatocytes for killing in vivo and contribute to protection elicited by whole-parasite vaccination.
Wang et al., Chongqing, China. In Plos One, 2013
Finally we showed that the use of heterologous prime/boost immunization strategies that use genetically attenuated parasites and DNA vaccines enabled the characterization of a novel pre-erythrocytic antigen, Tmp21, as a contributor to Pyfabb/f- induced protection.
Expression of tmp21 in normal adult human tissues.
Liu et al., Chongqing, China. In Int J Clin Exp Med, 2013
TMP21, known as p23 protein, is one important member of the p24 protein families.
The enterohemorrhagic Escherichia coli effector protein NleF binds mammalian Tmp21.
Hardwidge et al., Kansas City, United States. In Vet Microbiol, 2013
Using a yeast two-hybrid screen, we identified Tmp21, a type-I integral membrane protein and COPI-vesicle receptor involved in trans-Golgi network function, as an NleF-binding partner.
The role of TMP21 in trafficking and amyloid-β precursor protein (APP) processing in Alzheimer's disease.
Song et al., Vancouver, Canada. In Curr Alzheimer Res, 2012
This study suggested that The role ofTMP21 in the modulation of gamma-secretase activity and protein trafficking and related to alzheimer disease.
Assembly of the presenilin γ-/ε-secretase complex.
Fraser et al., Toronto, Canada. In J Neurochem, 2012
Several endogenous proteins have been reported to selectively modulate the function of the presenilin complexes; these include transmembrane trafficking protein, 21-KD (TMP21), CD147 antigen (basigin), the γ-secretase-activating protein (gSAP), and the orphan G-protein-coupled receptor 3. Because the structure and assembly of these complexes underlies their activity, this review will discuss current work on the assembly of the complex and on presenilin-interacting proteins that regulate secretase activity.
Tmp21, a novel MHC-I interacting protein, preferentially binds to Β2-microglobulin-free MHC-I heavy chains.
Ahn et al., Kwangju, South Korea. In Bmb Rep, 2011
Results suggest that Tmp21 is a novel protein that preferentially binds to Beta(2)-microglobulin-free MHC-I heavy chains.
p23/Tmp21 associates with protein kinase Cdelta (PKCdelta) and modulates its apoptotic function.
Kazanietz et al., Philadelphia, United States. In J Biol Chem, 2011
p23 acts as an anchoring protein that retains PKCdelta at the perinuclear region, thus limiting the availability of this kinase for activation in response to stimuli.
Proteinase-activated receptors, nucleotide P2Y receptors, and μ-opioid receptor-1B are under the control of the type I transmembrane proteins p23 and p24A in post-Golgi trafficking.
Reiser et al., Magdeburg, Germany. In J Neurochem, 2011
Transmembrane protein 23 and p24A differentially control G-protein coupled receptor trafficking and signaling in astrocytes.
Transgenic neuronal overexpression reveals that stringently regulated p23 expression is critical for coordinated movement in mice.
Thinakaran et al., Chicago, United States. In Mol Neurodegener, 2010
Data show that the level of p23 expression is critical for neuronal function, and p23 overexpression initiates a cascade in brainstem that leads to severe motor deficits and other neurological problems, culminating in premature death.
Transcriptional Regulation of TMP21 by NFAT.
Song et al., Chongqing, China. In Mol Neurodegener, 2010
BACKGROUND: TMP21 is a member of the p24 cargo protein family, which is involved in protein transport between the Golgi apparatus and ER.
Dilysine retrieval signal-containing p24 proteins collaborate in inhibiting γ-cleavage of amyloid precursor protein.
Nishimura et al., Ōtsu, Japan. In J Neurochem, 2010
Although the regulatory mechanism of γ-secretase cleavage remains unresolved, a member of the p24 cargo protein family, named p24δ(1) or TMP21, has been identified as an activity-modulating component.
The trafficking protein Tmed2/p24beta(1) is required for morphogenesis of the mouse embryo and placenta.
Lacy et al., Montréal, Canada. In Dev Biol, 2010
We find that Tmed2/p24beta(1) is normally expressed in tissues showing morphological defects in 99J mutant embryos and that these affected tissues lack the TMED2/p24beta(1) oligomerization partners, TMED7/p24gamma(3) and TMED10/p24delta(1).
p23/Tmp21 differentially targets the Rac-GAP beta2-chimaerin and protein kinase C via their C1 domains.
Kazanietz et al., Philadelphia, United States. In Mol Biol Cell, 2010
These results demonstrate that p23/Tmp21 acts as an anchor that distinctively modulates compartmentalization of C1 domain-containing proteins, and it plays an essential role in beta2-chimaerin relocalization.
TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity.
Fraser et al., Toronto, Canada. In Nature, 2006
TMP21, a member of the p24 cargo protein family, is a component of presenilin complexes and differentially regulates gamma-secretase cleavage without affecting epsilon-secretase activity
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