Sec23 Homolog A (S. Cerevisiae) Proteine (SEC23A)

Mouse (Murine) Sec23 Homolog A (S. Cerevisiae) (SEC23A) Interaktionspartner

1. these data demonstrate an equivalent function for SEC23A/B, with evolutionary shifts in the transcription program likely accounting for the distinct phenotypes of SEC23A/B deficiency within and across species, a paradigm potentially applicable to other sets of paralogous genes.

2. This study also validated the interaction between HAP1 and Sec23A using co-immunoprecipitation experiments with endogenous proteins. This manuscript also reports on the high confidence interacting partners of HAP1 identified by the non-biased approach used in this study, which interestingly, consists of predominantly trafficking-related proteins

3. results suggest that mammalian SEC23A and SEC23B transport overlapping yet distinct spectra of cargo in vivo

4. Sec23a contains consensus TFII-I binding sites in the proximal promoters; the chromatin immunoprecipitation analysis showed that TFII-I transcription factors are recruited to these sites in vivo in Williams-Beuren syndrome.

5. Regulation of endoplasmic reticulum stress response by a BBF2H7-mediated Sec23a pathway is essential for chondrogenesis.

Zebrafish Sec23 Homolog A (S. Cerevisiae) (SEC23A) Interaktionspartner

1. sec23b is an essential component of the cartilage extracellular matrix secretory pathway in chondrocytes

Human Sec23 Homolog A (S. Cerevisiae) (SEC23A) Interaktionspartner

1. identified Sec23a, a gene target of miR-200c, suppresses miR-200c augmented oligometastatic to polymetastatic progression via its secretome. Firstly, miR-200c over-expression and Sec23a interference accelerated oligometastatic to polymetatic progression. Secondly, Sec23a functions downstream of miR-200c.

2. This larger GWAS yields two loci harboring genome-wide significant variants affecting serum 25-hydroxyvitamin D levels (P = 4.7x10(-9) at rs8018720 in SEC23A, and P = 1.9x10(-14) at rs10745742 in AMDHD1).

3. these data demonstrate an equivalent function for SEC23A/B, with evolutionary shifts in the transcription program likely accounting for the distinct phenotypes of SEC23A/B deficiency within and across species, a paradigm potentially applicable to other sets of paralogous genes.

4. Mutation on serine207 of Sec23A protein changes Unc-51 like kinase 1(ULK 1) targeted phosphorylation. During elevated autophagy, induced by amino acid starvation, rapamycin, or overexpression of ULK1,phosphorylation of Sec23A reduced the interaction between vesicular transport proteins Sec23A and Sec31A.

5. Data indicate that vesicular transport protein SEC23A as a target of miR-375.

6. findings suggest that miR-21 promoted proliferation, migration, and invasion of colorectal cancer cells in vitro by down regulating the expression of Sec23A

7. miR-375 is involved in development of chemo-resistance to docetaxel through regulating SEC23A and YAP1 expression.

8. ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex.

9. Hypomorphic mutations of SEC23B gene account for mild phenotypes of congenital dyserythropoietic anemia type II.

10. show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER

11. Data indicate that a synthetic polypeptide containing the N terminus of bovine AE1 bound the Sec23A-Sec24C complex through a selective interaction with Sec24C.

12. the BBF2H7-mediated Sec23A pathway is required for ER-to-Golgi procollagen trafficking to promote collagen synthesis

13. Sec23A overexpression reduced cell growth but did not induce apoptosis, whereas inhibition of Sec23A stimulated cell proliferation

14. When entering into mitosis, the COPII component Sec24Cp is simultaneously deglycosylated and phosphorylated; however, Sec23A is not.

15. Sec23A mutation causes cranio-lenticulo-sutural dysplasia, and disrupts the nucleation of COPII coat proteins at endoplasmic reticulum exit sites.

16. Data show that coupling of the Sec23/24 and Sec13/31 layers of the COPII coat is required to drive export of collagen from the endoplasmic reticulum, and that efficient COPII assembly is essential for normal craniofacial development during embryogenesis.