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Results show the crystal structure of the complex between ALG-2 (show PDCD6 Proteins) and a peptide of Sec31A and found that the peptide binds to the third hydrophobic pocket (Pocket 3) and that ALG-2 (show PDCD6 Proteins) recognizing 2 types of motifs at different hydrophobic surfaces of Sec31A.
findings suggest that AnxA11 (show ANXA11 Proteins) maintains architectural and functional features of the ERES by coordinating with ALG-2 (show PDCD6 Proteins) to stabilize Sec31A at the ERES.
ALG-2/Sec31A interactions were not required for the localization of Sec31A to ER exit sites per se but appeared to acutely regulate the stability and trafficking of the cargo receptor p24 and the distribution of the vesicle tether protein p115
ALG-2 (show PDCD6 Proteins) attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex.
These results suggest that Sec31 (show EXOC1 Proteins) phosphorylation by CK2 (show CSNK2A1 Proteins) controls the duration of COPII vesicle formation, which regulates ER-to-Golgi trafficking.
efficient COPII-dependent secretion, notably assembly of Sec13 (show SEC13 Proteins)-Sec31 (show EXOC1 Proteins), is required to drive epithelial morphogenesis in both two- and three-dimensional cultures
SEC31A-ALK fusions are recurrent in ALK-positive large B-cell lymphomas.
t(4;9)(q21;p24) leads to a novel SEC31A-JAK2 (show JAK2 Proteins) fusion in Hodgkin lymphoma
the alg2 (show PDCD6 Proteins) binding site is one of the key determinants of the retention kinetics of Sec31A at endoplasmic reticulum exit sites
Genomic PCR and subsequent sequencing showed that the breakpoints were located in intron 23 of SEC31L1 and intron 20 of anaplastic lymphoma kinase
efficient COPII-dependent secretion, notably assembly of Sec13 (show SEC13 Proteins)-Sec31 (show EXOC1 Proteins), is required to drive epithelial morphogenesis
Data show that coupling of Sec23/24 and Sec13 (show SEC13 Proteins)/31 layers of the COPII coat (show SEC23A Proteins) is required to drive export of collagen from the endoplasmic reticulum, and that COPII assembly is essential for normal craniofacial development during embryogenesis.
The protein encoded by this gene is similar to yeast Sec31 protein. Yeast Sec31 protein is known to be a component of the COPII protein complex which is responsible for vesicle budding from endoplasmic reticulum (ER). This protein was found to colocalize with SEC13, one of the other components of COPII , in the subcellular structures corresponding to the vesicle transport function. An immunodepletion experiment confirmed that this protein is required for ER-Golgi transport. Alternative splicing results in multiple transcript variants encoding different isoforms.
SEC31-like protein 1
, SEC31-related protein A
, protein transport protein Sec31A
, web1-like protein
, yeast Sec31p homolog
, SEC31-like 1
, vesicle associated protein
, vesicle-associated protein 1
, sec31p homolog