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    PDCD6 programmed cell death 6 [ Homo sapiens (human) ]

    Gene ID: 10016, updated on 5-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The Contribution of PDCD6 Polymorphisms to Oral Cancer Risk.

    The Contribution of PDCD6 Polymorphisms to Oral Cancer Risk.
    Shih LC, He JL, Chang WS, Hsu CL, Hsia TC, Wang YC, Yang JS, Mong MC, Tsai CW, Bau DT., Free PMC Article

    07/2/2022
    ALG2 regulates type I interferon responses by inhibiting STING trafficking.

    ALG2 regulates type I interferon responses by inhibiting STING trafficking.
    Ji W, Zhang L, Xu X, Liu X.

    04/30/2022
    Expression level of NEAT1 differentiates benign and malignant thyroid nodules by regulating NEAT1/miR9/PTEN and NEAT1/miR124/PDCD6 signalling.

    Expression level of NEAT1 differentiates benign and malignant thyroid nodules by regulating NEAT1/miR‑9/PTEN and NEAT1/miR‑124/PDCD6 signalling.
    Zhao L, Zhou N, Zhao P., Free PMC Article

    07/3/2021
    PDCD6 cooperates with C-Raf to facilitate colorectal cancer progression via Raf/MEK/ERK activation.

    PDCD6 cooperates with C-Raf to facilitate colorectal cancer progression via Raf/MEK/ERK activation.
    Wang X, Wu F, Wang H, Duan X, Huang R, Tuersuntuoheti A, Su L, Yan S, Zhao Y, Lu Y, Li K, Yao J, Luo Z, Guo L, Liu J, Chen X, Lu Y, Hu H, Li X, Bao M, Bi X, Du B, Miao S, Cai J, Wang L, Zhou H, Ying J, Song W, Zhao H., Free PMC Article

    05/1/2021
    ALG-2 couples T cell activation and apoptosis by regulating proteasome activity and influencing MCL1 stability.

    ALG-2 couples T cell activation and apoptosis by regulating proteasome activity and influencing MCL1 stability.
    He TS, Ji W, Zhang J, Lu J, Liu X., Free PMC Article

    11/21/2020
    The low expression of miR-124 can promote the proliferation as well as migration of esophageal cancer cells and inhibit cell apoptosis. The mechanism may be that miR-124 can regulate the expression of PDCD6.

    Highly expressed microRNA-124 inhibits migration and promotes apoptosis of esophageal cancer cells by degrading PDCD6.
    Hu S, Zang R, Wang Y, Liang Y, Mu J, Zhang Y, Ma J.

    11/23/2019
    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

    Adaptor functions of the Ca(2+)-binding protein ALG-2 in protein transport from the endoplasmic reticulum.
    Shibata H.

    02/2/2019
    Up-regulation of miR-20a by HPV16 E6 exerted growth-promoting effects by targeting PDCD6 in cervical carcinoma cells.

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

    10/6/2018
    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-.

    RUNX1-PDCD6 fusion resulting from a novel t(5;21)(p15;q22) chromosome translocation in myelodysplastic syndrome secondary to chronic lymphocytic leukemia.
    Panagopoulos I, Gorunova L, Jacobsen EM, Andersen K, Micci F, Heim S., Free PMC Article

    07/28/2018
    ALG-2 binding to Scotin is strictly calcium dependent, indicating a role of this interaction in calcium signaling pathways

    The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane.
    Draeby I, Woods YL, la Cour JM, Mollerup J, Bourdon JC, Berchtold MW., Free PMC Article

    05/31/2018
    Ca2+-loaded ALG-2 bridges Alix and TSG101 as an adaptor protein.

    Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101.
    Okumura M, Ichioka F, Kobayashi R, Suzuki H, Yoshida H, Shibata H, Maki M.

    05/31/2018
    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

    Simultaneous targeting of Requiem & Alg-2 in Chinese hamster ovary cells for improved recombinant protein production.
    Lim Y, Mantalaris A, Yap MG, Wong DC.

    05/31/2018
    inability of the two-residue shorter ALG-2 isoform to bind Alix

    Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition.
    Inuzuka T, Suzuki H, Kawasaki M, Shibata H, Wakatsuki S, Maki M., Free PMC Article

    05/31/2018
    the alg2 binding site is one of the key determinants of the retention kinetics of Sec31A at endoplasmic reticulum exit sites

    The ALG-2 binding site in Sec31A influences the retention kinetics of Sec31A at the endoplasmic reticulum exit sites as revealed by live-cell time-lapse imaging.
    Shibata H, Inuzuka T, Yoshida H, Sugiura H, Wada I, Maki M.

    05/31/2018
    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.

    Identification of the P-body component PATL1 as a novel ALG-2-interacting protein by in silico and far-Western screening of proline-rich proteins.
    Osugi K, Suzuki H, Nomura T, Ariumi Y, Shibata H, Maki M.

    05/31/2018
    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

    VPS37 isoforms differentially modulate the ternary complex formation of ALIX, ALG-2, and ESCRT-I.
    Okumura M, Katsuyama AM, Shibata H, Maki M.

    05/31/2018
    ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex.

    ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex.
    la Cour JM, Schindler AJ, Berchtold MW, Schekman R., Free PMC Article

    05/31/2018
    Lack of ALG-2, ALIX or Vps4B each prevents shedding, and repair of the injured cell membrane

    Mechanism of Ca²⁺-triggered ESCRT assembly and regulation of cell membrane repair.
    Scheffer LL, Sreetama SC, Sharma N, Medikayala S, Brown KJ, Defour A, Jaiswal JK., Free PMC Article

    05/31/2018
    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.

    Structural analysis of the complex between penta-EF-hand ALG-2 protein and Sec31A peptide reveals a novel target recognition mechanism of ALG-2.
    Takahashi T, Kojima K, Zhang W, Sasaki K, Ito M, Suzuki H, Kawasaki M, Wakatsuki S, Takahara T, Shibata H, Maki M., Free PMC Article

    05/31/2018
    Alix and ALG-2 are new actors of the TNF-R1 pathway

    Alix and ALG-2 are involved in tumor necrosis factor receptor 1-induced cell death.
    Mahul-Mellier AL, Strappazzon F, Petiot A, Chatellard-Causse C, Torch S, Blot B, Freeman K, Kuhn L, Garin J, Verna JM, Fraboulet S, Sadoul R., Free PMC Article

    05/31/2018
    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.

    ALG-2 knockdown in HeLa cells results in G2/M cell cycle phase accumulation and cell death.
    Høj BR, la Cour JM, Mollerup J, Berchtold MW.

    05/31/2018
    analysed the expression of ALG-2 in 7371 tumor tissue samples of various origin; most notably, ALG-2 was upregulated in mesenchymal tumors.

    The apoptosis linked gene ALG-2 is dysregulated in tumors of various origin and contributes to cancer cell viability.
    la Cour JM, Høj BR, Mollerup J, Simon R, Sauter G, Berchtold MW., Free PMC Article

    05/31/2018
    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

    Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: a potential effector pathway for luminal calcium.
    Helm JR, Bentley M, Thorsen KD, Wang T, Foltz L, Oorschot V, Klumperman J, Hay JC., Free PMC Article

    05/31/2018
    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.

    Apoptosis-linked gene 2 promotes breast cancer growth and metastasis by regulating the cytoskeleton.
    Qin J, Li D, Zhou Y, Xie S, Du X, Hao Z, Liu R, Liu X, Liu M, Zhou J., Free PMC Article

    05/31/2018
    MAP1B heavy chain has a unique binding site for a calcium-binding protein ALG-2.

    A microtubule-associated protein MAP1B binds to and regulates localization of a calcium-binding protein ALG-2.
    Takahara T, Arai Y, Kono Y, Shibata H, Maki M.

    04/7/2018
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