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SEC22 vesicle trafficking protein homolog B

Sec22b, ERS-24, mSec22b
The protein encoded by this gene is a member of the SEC22 family of vesicle trafficking proteins. It seems to complex with SNARE and it is thought to play a role in the ER-Golgi protein trafficking. This protein has strong similarity to Mus musculus and Cricetulus griseus proteins.[provided by RefSeq, Sep 2009] (from NCBI)
Top mentioned proteins: CAN, BET1, v-SNARE, HAD, STEP
Papers on Sec22b
p115-SNARE interactions: a dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles.
Hay et al., Missoula, United States. In Traffic, Feb 2015
Using a gel filtration binding assay, we have demonstrated that in solution p115 stably interacts with ER/Golgi SNAREs rbet1 and sec22b, but not membrin and syntaxin 5.
Disruption of the fusion of Leishmania parasitophorous vacuoles with ER vesicles results in the control of the infection.
Kima et al., Gainesville, United States. In Cell Microbiol, 2012
In the presence of dominant negative variants of sec22b or some of its known cognate partners, D12 and syntaxin 18, PVs failed to distend and harboured fewer parasites.
The pathway of cross-presentation is influenced by the particle size of phagocytosed antigen.
Williams et al., Southampton, United Kingdom. In Immunology, 2012
Whereas early endosome autoantigen 1 (EEA1) could be observed in all phagosomes, we observed endoplasmic reticulum SNARE of molecular weight 24 000 (ERS24) and cathepsin S in association with 3·0-μm and aggregated 0·8-μm MS, but not individual 0·8-μm MS.
The Legionella pneumophila effector DrrA is sufficient to stimulate SNARE-dependent membrane fusion.
Roy et al., New Haven, United States. In Cell Host Microbe, 2012
DrrA activation of the Rab1 GTPase on plasma membrane-derived organelles stimulated the tethering of endoplasmic reticulum-derived vesicles, resulting in vesicle fusion through the pairing of Sec22b with the plasma membrane syntaxin proteins.
Sec22b regulates phagosomal maturation and antigen crosspresentation by dendritic cells.
Savina et al., Paris, France. In Cell, 2012
Findings provide insight into an intracellular traffic pathway required for crosspresentation and show that Sec22b-dependent recruitment of endoplasmic reticulum proteins to phagosomes critically influences phagosomal functions in dendritic cells.
Identification of host factors involved in coronavirus replication by quantitative proteomics analysis.
de Haan et al., Utrecht, Netherlands. In Proteomics, 2011
Transfection of small interfering RNAs targeting either C11orf59 or Golgi apparatus glycoprotein 1 resulted in increased virus replication, whereas depletion of vesicle-trafficking protein vesicle-trafficking protein sec22b enhanced the release of infectious progeny virus.
Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs.
Hay et al., Missoula, United States. In Mol Biol Cell, 2010
Ykt6 reversed alpha-synuclein inhibition much more effectively than sec22b, suggesting a possible neuroprotective role for the enigmatic high expression of ykt6 in neurons.
Sec22b is a negative regulator of phagocytosis in macrophages.
Wada et al., Fukushima, Japan. In Mol Biol Cell, 2009
The R-SNARE motif, a selective domain for forming a SNARE complex with syntaxin18 and/or D12, was responsible for the inhibition of phagocytosis. Sec22b is a negative regulator of phagocytosis in macrophages by regulating free syntaxin 18 and/or D12.
Members of a mammalian SNARE complex interact in the endoplasmic reticulum in vivo and are found in COPI vesicles.
Söling et al., Göttingen, Germany. In Eur J Cell Biol, 2008
Here, we report that the mammalian soluble N-ethylmaleimide-sensitive factor (NSF) attachment receptor (SNARE) proteins mSec22b, mUse1/D12, mSec20/BNIP1, and syntaxin 18 form a quaternary SNARE complex.
Evidence for regulation of ER/Golgi SNARE complex formation by hsc70 chaperones.
Hay et al., Ann Arbor, United States. In Eur J Cell Biol, 2005
Here we demonstrate that hsc70 chaperones stimulate in vitro SNARE complex formation among the ER/Golgi SNAREs syntaxin 5, membrin, rbetl and sec22b, under conditions in which assembly is normally inhibited.
Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages.
Rothman et al., New York City, United States. In Proc Natl Acad Sci U S A, 2005
Here we report that direct ER-plasma membrane fusion during phagocytosis requires the ER resident soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein ERS24/Sec22b and that J774-macrophages react toward the challenge of large (3.0-microm) but not small (0.8-microm) particles by triggering this fusion mechanism, allowing them to access the most abundant endogenous membrane source in the cell, the ER.
The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling.
Sacher et al., Montréal, Canada. In J Biol Chem, 2004
Both proteins also share structural similarity with the amino-terminal regulatory domains of the membrane trafficking proteins, sec22b and Ykt6p, as well as with sedlin (a component of a Golgi-associated membrane-trafficking complex) and the sigma2 and amino-terminal portion of the mu2 subunits of the clathrin adaptor complex AP2.
Countercurrent distribution of two distinct SNARE complexes mediating transport within the Golgi stack.
Orci et al., Genève, Switzerland. In Mol Biol Cell, 2004
This contrasts with a second distinct SNARE complex, also required for intra-Golgi transport, consisting of syntaxin 5 (Sed5)-membrin (Bos1)-ERS24 (Sec22)-rBet1 (Bet1), whose v-(rBet1) and t-SNARE subunits (membrin and ERS24), progressively decrease in concentration toward the trans face.
The SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactions.
Hay et al., Ann Arbor, United States. In J Biol Chem, 2003
We utilized protein interaction assays to demonstrate that the rbet1 SNARE motif plays a structural role similar to the carboxyl-terminal helix of SNAP-25 in the synaptic SNARE complex and demonstrated the importance to SNARE complex assembly of a conserved salt bridge between rbet1 and sec22b.
A novel snare N-terminal domain revealed by the crystal structure of Sec22b.
Scheller et al., Stanford, United States. In J Biol Chem, 2001
To better understand this regulation, we have determined the 2.4-A crystal structure of the 130-amino acid N-terminal domain of mouse Sec22b (mSec22b), a SNARE involved in endoplasmic reticulum/Golgi membrane trafficking.
Subunit structure of a mammalian ER/Golgi SNARE complex.
Hay et al., Ann Arbor, United States. In J Biol Chem, 2001
Purified recombinant syntaxin 5, membrin, and rbet1, three Q-SNAREs, assemble cooperatively to create a high affinity binding site for sec22b, an R-SNARE.
Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment.
Hong et al., Singapore, Singapore. In Mol Biol Cell, 1999
Three mammalian proteins homologous to Sec22p have been identified and are referred to as Sec22a, Sec22b/ERS-24, and Sec22c, respectively.
Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells.
Scheller et al., Stanford, United States. In Cell, 1997
The proposed cis-Golgi vesicle receptor syntaxin 5 was found in a complex with Golgi-associated SNARE of 28 kDa (GOS-28), rbet1, rsly1, and two novel proteins characterized herein: rat sec22b and membrin, both cytoplasmically oriented integral membrane proteins.
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