gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Lectin, mannose-binding, 1

ERGIC-53, LMAN1, F5F8D, gp58
The protein encoded by this gene is a type I integral membrane protein localized in the intermediate region between the endoplasmic reticulum and the Golgi, presumably recycling between the two compartments. The protein is a mannose-specific lectin and is a member of a novel family of plant lectin homologs in the secretory pathway of animal cells. Mutations in the gene are associated with a coagulation defect. Using positional cloning, the gene was identified as the disease gene leading to combined factor V-factor VIII deficiency, a rare, autosomal recessive disorder in which both coagulation factors V and VIII are diminished. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CD45, MCFD2, FVIII, CIs, ACID
Papers on ERGIC-53
Release of Vesicular Stomatitis Virus Spike Protein G-Pseudotyped Lentivirus from the Host Cell Is Impaired upon Low-Density Lipoprotein Receptor Overexpression.
Blaas et al., Vienna, Austria. In J Virol, Dec 2015
Intracellular VSVG granules colocalized with LDLR, ER-Golgi intermediate compartment protein 53 (ERGIC53), LAMP2, and vimentin but not with GM130 or calnexin, suggesting that VSVG interacts with LDLR within the ERGIC, resulting in rerouting into the aggresome/autophagosome pathway.
Congenital factor V and VIII deficiency in women: a systematic review of literature and report of two new cases.
Kadir et al., London, United Kingdom. In Blood Coagul Fibrinolysis, Oct 2015
UNASSIGNED: Factor V and factor VIII deficiency (F5F8D) is a rare congenital bleeding disorder.
LMAN1 (ERGIC-53) is a potential carrier protein for matrix metalloproteinase-9 glycoprotein secretion.
Yang et al., Madison, United States. In Biochem Biophys Res Commun, Sep 2015
Through a complementation assay, we determined that LMAN1, a well-studied lectin-carrier protein, interacts with a secretion-competent N-glycosylated MMP-9 in the ER while N-glycosylation-deficient secretion-compromised MMP-9 does not.
Congenital combined deficiency of coagulation factors: a study of seven patients.
Dorgalaleh et al., Sārī, Iran. In Blood Coagul Fibrinolysis, 2015
Among 358 patients, four were found to be affected with combined factor (F)V and FVIII deficiency (F5F8D).
Interaction of early secretory pathway and Golgi membranes with microtubules and microtubule motors.
Nadezhdina et al., Moscow, Russia. In Biochemistry (mosc), 2014
Movement of vesicles in cells containing the intermediate compartment protein ERGIC53/LMANI was inhibited by inhibiting dynein.
VAP-B binds to Rab3GAP1 at the ER: its implication in nuclear envelope formation through the ER-Golgi intermediate compartment.
Sakisaka et al., Kōbe, Japan. In Kobe J Med Sci, 2013
On the other hand, the FFAT-like motif mutation increases the binding activity of Rab3GAP1 to ERGIC-53, the ERGIC marker protein.
Combined deficiency of coagulation factors V and VIII: an update.
Zhang et al., Cleveland, United States. In Semin Thromb Hemost, 2013
Disrupting the LMAN1-MCFD2 receptor, complex formation is the primary molecular defect of missense mutations leading to F5F8D.
The COPII pathway and hematologic disease.
Ginsburg et al., Ann Arbor, United States. In Blood, 2012
F5F8D results from mutations in either LMAN1 (lectin mannose-binding protein 1) or MCFD2 (multiple coagulation factor deficiency protein 2), which encode the ER cargo receptor complex LMAN1-MCFD2.
Protein interaction profiling of the p97 adaptor UBXD1 points to a role for the complex in modulating ERGIC-53 trafficking.
Deshaies et al., Philadelphia, United States. In Mol Cell Proteomics, 2012
UBXD1 modulates the trafficking of ERGIC-53-containing vesicles by controlling the interaction of transport factors with the cytoplasmic tail of ERGIC-53.
Two new mutations at ERGIC-53 gene in a Turkish family.
Akar et al., Ankara, Turkey. In Clin Appl Thromb Hemost, 2011
Two new mutations at ERGIC-53 gene in a Turkish family.
Inherited and acquired factor V deficiency.
Franchini et al., Parma, Italy. In Blood Coagul Fibrinolysis, 2011
The combined deficiency of factor V and FVIII, commonly known as F5F8D, is a recessive disorder not attributable to the association of isolated factor V and FVIII deficiencies, but rather to defective intracellular processing of both proteins due to mutations involving the LMAN1 and MCFD2 genes, which encode two proteins forming an essential cargo receptor complex.
Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII.
Lindqvist et al., Stockholm, Sweden. In Febs Lett, 2010
Data present the crystal structure of the LMAN1/MCFD2 complex and relate it to patient mutations. Circular dichroism data show that the majority of the substitution mutations give rise to a disordered or severely destabilized MCFD2 protein.
EF-hand domains of MCFD2 mediate interactions with both LMAN1 and coagulation factor V or VIII.
Zhang et al., Cleveland, United States. In Blood, 2010
Data show that mutations in MCFD2 that disrupt the tertiary structure and abolish LMAN1 binding still retain the FV/FVIII binding activities, suggesting that this interaction is independent of Ca(2+)-induced folding of the protein.
Chemical approaches toward understanding glycan-mediated protein quality control.
Ito et al., Wako, Japan. In Curr Opin Chem Biol, 2009
Involved in this process are a number of intracellular carbohydrate-recognizing proteins or carbohydrate-processing enzymes, including calnexin/calreticulin, malectin, glucosidase I (G-I) and II (G-II), UDP-glucose:glycoprotein glucosyltransferase (UGGT), cargo receptors (VIP36, ERGL, and ERGIC-53), ER 1,2-mannosidase I, ER degradation-enhancing alpha-mannosidase-like proteins (EDEMs) and ubiquitin ligase.
Macrophage-specific expression of mannose-binding lectin controls atherosclerosis in low-density lipoprotein receptor-deficient mice.
Buurman et al., Maastricht, Netherlands. In Circulation, 2009
MBL deposition and gene expression in advanced human atherosclerotic lesions revealed the presence of MBL protein in ruptured but not stable atherosclerotic lesions
Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex.
Ginsburg et al., Ann Arbor, United States. In Nat Genet, 2003
inactivating mutations in MCFD2 cause combined deficiency of factor V and factor VIII with a phenotype indistinguishable from that caused by mutations in LMAN1
Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum.
Pepperkok et al., Heidelberg, Germany. In Nat Cell Biol, 1999
Microinjection of anti-COP-I antibodies inhibits retrieval of the lectin-like molecule ERGIC-53 and of the KDEL receptor from the Golgi to the ER.
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
Hauri et al., Basel, Switzerland. In Nat Cell Biol, 1999
Here we show that a cathepsin-Z-related glycoprotein binds to the recycling, mannose-specific membrane lectin ERGIC-53.
Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII.
Ginsburg et al., Ann Arbor, United States. In Cell, 1998
ERGIC-53, a component of the ER-Golgi intermediate compartment, was mapped to a YAC and BAC contig containing the critical region for the combined factors V and VIII deficiency gene.
Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI.
Kreis et al., Genève, Switzerland. In Cell, 1997
Upon shifting to permissive temperature, ts-G-GFP(ct) concentrates into COPII-positive structures close to the ER, which then build up to form an intermediate compartment or transport complex, containing ERGIC-53 and the KDEL receptor, where COPII is replaced by COPI.
share on facebooktweetadd +1mail to friends