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Human Programmed Cell Death 6 (PDCD6) interaction partners

1. ALG-2 is predominantly localized to a specialized region of the endoplasmic reticulum (ER), called the ER exit site (ERES), through its interaction with Sec31A. Sec31A is an outer coat protein of coat protein complex II (COPII) and is recruited from the cytosol to the ERES to form COPII-coated transport vesicles

2. Up-regulation of miR-20a by HPV16 E6 exerted growth-promoting effects by targeting PDCD6 in cervical carcinoma cells.

3. the t(5;21)(p15;q22) translocation could be identified only when what had seemed like a del(21)(qq) in G-banded preparations was examined using FISH and RNA-sequencing directed at finding out what lay behind the 21q-.

4. ALG-2 binding to Scotin is strictly calcium dependent, indicating a role of this interaction in calcium signaling pathways

5. Ca2+-loaded ALG-2 bridges Alix and TSG101 as an adaptor protein.

6. found that targeting Requiem and Alg-2 did not result in extended culture viability, but resulted in an increase in maximum viable cell numbers and cumulative IVCD under fed-batch conditions

7. inability of the two-residue shorter ALG-2 isoform to bind Alix

8. the alg2 binding site is one of the key determinants of the retention kinetics of Sec31A at endoplasmic reticulum exit sites

9. This is the first report showing interaction of ALG-2 with a P-body component (PATL1).PATL1 as well as DCP1A, a well-known P-body marker, co-localized with a subset of ALG-2.

10. The results of in vitro binding assays using purified recombinant proteins indicated that ALG-2 functions as a Ca(2)-dependent adaptor protein that bridges ALIX and ESCRT-I to form a ternary complex

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

12. Lack of ALG-2, ALIX or Vps4B each prevents shedding, and repair of the injured cell membrane

13. Results show the crystal structure of the complex between ALG-2 and a peptide of Sec31A and found that the peptide binds to the third hydrophobic pocket (Pocket 3) and that ALG-2 recognizing 2 types of motifs at different hydrophobic surfaces of Sec31A.

14. Alix and ALG-2 are new actors of the TNF-R1 pathway

15. These results indicate that ALG-2 has an anti-apoptotic function in HeLa cells by facilitating the passage through checkpoints in the G2/M cell cycle phase.

16. analysed the expression of ALG-2 in 7371 tumor tissue samples of various origin; most notably, ALG-2 was upregulated in mesenchymal tumors.

17. 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

18. Our study demonstrates that ALG-2 plays a role in the regulation of cytoskeletal rearrangement that drives cell polarization and migration in breast cancer cells.

19. MAP1B heavy chain has a unique binding site for a calcium-binding protein ALG-2.

20. These results suggest that a change in the intracellular calcium level plays a role in regulation of the secretory pathway via interaction of ALG-2 with MISSL and MAP1B.

Mouse (Murine) Programmed Cell Death 6 (PDCD6) interaction partners

1. Results provide a better understanding of the target recognition mechanism and conformational change of SOUL in the interaction with ALG-2.

2. ALG2 regulates glioblastoma cell proliferation, migration and tumorigenicity.

3. Substitution of either L52 with Ala or F148 with Ser of ALG-2 caused loss of binding abilities to PLSCR3 lacking type 1 motif but retained those to PLSCR3 lacking type 2 motif

4. ALG-2 is physiologically dispensable for apoptotic responses (ALG-2 protein)