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    DCLRE1B DNA cross-link repair 1B [ Homo sapiens (human) ]

    Gene ID: 64858, updated on 19-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    DNA-PK controls Apollo's access to leading-end telomeres.

    DNA-PK controls Apollo's access to leading-end telomeres.
    Sonmez C, Toia B, Eickhoff P, Matei AM, El Beyrouthy M, Wallner B, Douglas ME, de Lange T, Lottersberger F., Free PMC Article

    05/30/2024
    DCLRE1B/Apollo germline mutations associated with renal cell carcinoma impair telomere protection.

    DCLRE1B/Apollo germline mutations associated with renal cell carcinoma impair telomere protection.
    Bories C, Lejour T, Adolphe F, Kermasson L, Couvé S, Tanguy L, Luszczewska G, Watzky M, Poillerat V, Garnier P, Groisman R, Ferlicot S, Richard S, Saparbaev M, Revy P, Gad S, Renaud F.

    05/6/2024
    DCLRE1B promotes tumor progression and predicts immunotherapy response through METTL3-mediated m6A modification in pancreatic cancer.

    DCLRE1B promotes tumor progression and predicts immunotherapy response through METTL3-mediated m6A modification in pancreatic cancer.
    Li L, Wang F, Deng Z, Zhang G, Zhu L, Zhao Z, Liu R., Free PMC Article

    11/14/2023
    Structural and mechanistic insights into the Artemis endonuclease and strategies for its inhibition.

    Structural and mechanistic insights into the Artemis endonuclease and strategies for its inhibition.
    Yosaatmadja Y, Baddock HT, Newman JA, Bielinski M, Gavard AE, Mukhopadhyay SMM, Dannerfjord AA, Schofield CJ, McHugh PJ, Gileadi O., Free PMC Article

    11/6/2021
    A phosphate binding pocket is a key determinant of exo- versus endo-nucleolytic activity in the SNM1 nuclease family.

    A phosphate binding pocket is a key determinant of exo- versus endo-nucleolytic activity in the SNM1 nuclease family.
    Baddock HT, Newman JA, Yosaatmadja Y, Bielinski M, Schofield CJ, Gileadi O, McHugh PJ., Free PMC Article

    11/6/2021
    Different charge distributions along the DNA binding groove may account for the drastic difference in processivity and DNA digestion efficiency, including that of damaged substrates, between SNM1A and SNM1B.

    The structures of the SNM1A and SNM1B/Apollo nuclease domains reveal a potential basis for their distinct DNA processing activities.
    Allerston CK, Lee SY, Newman JA, Schofield CJ, McHugh PJ, Gileadi O., Free PMC Article

    06/28/2016
    The SNM1B/APOLLO DNA nuclease functions in resolution of replication stress and maintenance of common fragile site stability.

    The SNM1B/APOLLO DNA nuclease functions in resolution of replication stress and maintenance of common fragile site stability.
    Mason JM, Das I, Arlt M, Patel N, Kraftson S, Glover TW, Sekiguchi JM., Free PMC Article

    07/26/2014
    the N-terminal region of Snm1B forms a complex containing PSF2 and Mus81, while the C-terminal region is important for PSF2-mediated chromatin association.

    Snm1B interacts with PSF2.
    Stringer JR, Counter CM., Free PMC Article

    05/18/2013
    The nuclease hSNM1B/Apollo is linked to the Fanconi anemia pathway via its interaction with FANCP/SLX4.

    The nuclease hSNM1B/Apollo is linked to the Fanconi anemia pathway via its interaction with FANCP/SLX4.
    Salewsky B, Schmiester M, Schindler D, Digweed M, Demuth I.

    03/30/2013
    differences in the substrate selectivities of SNM1A and SNM1B are likely to be relevant to their in vivo roles

    Characterization of the human SNM1A and SNM1B/Apollo DNA repair exonucleases.
    Sengerová B, Allerston CK, Abu M, Lee SY, Hartley J, Kiakos K, Schofield CJ, Hartley JA, Gileadi O, McHugh PJ., Free PMC Article

    10/13/2012
    SNM1B functions epistatically to the central Fanconi anemia factor, FANCD2, in cellular survival after interstrand crosslinks damage and homology-directed repair of DNA double-strand breaks

    Snm1B/Apollo functions in the Fanconi anemia pathway in response to DNA interstrand crosslinks.
    Mason JM, Sekiguchi JM., Free PMC Article

    10/22/2011
    TRF2, which binds preferentially to positively supercoiled DNA substrates, together with Apollo, negatively regulates the amount of TOP1, TOP2alpha, and TOP2beta at telomeres.

    TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage.
    Ye J, Lenain C, Bauwens S, Rizzo A, Saint-Léger A, Poulet A, Benarroch D, Magdinier F, Morere J, Amiard S, Verhoeyen E, Britton S, Calsou P, Salles B, Bizard A, Nadal M, Salvati E, Sabatier L, Wu Y, Biroccio A, Londoño-Vallejo A, Giraud-Panis MJ, Gilson E.

    08/23/2010
    DCLRE1B protein binds to a C-terminal fragment of HSP72 Heat-Shock Proteins, known to contain the substrate binding domain.

    Evidence for hSNM1B/Apollo functioning in the HSP70 mediated DNA damage response.
    Anders M, Mattow J, Digweed M, Demuth I.

    01/21/2010
    Results suggest that SNM1B/Apollo and Astrin function together to enforce the prophase checkpoint in response to spindle stress.

    SNM1B/Apollo interacts with astrin and is required for the prophase cell cycle checkpoint.
    Liu L, Akhter S, Bae JB, Mukhopadhyay SS, Richie CT, Liu X, Legerski R.

    01/21/2010
    observations suggest an important role for hSNM1B in the response to ionizing radiation damage, a role that may be, in part, upstream of the central player in maintenance of genome integrity, ATM

    Endogenous hSNM1B/Apollo interacts with TRF2 and stimulates ATM in response to ionizing radiation.
    Demuth I, Bradshaw PS, Lindner A, Anders M, Heinrich S, Kallenbach J, Schmelz K, Digweed M, Meyn MS, Concannon P., Free PMC Article

    01/21/2010
    The protein hSnm1B is stabilized when bound to the telomere-binding protein TRF2

    The protein hSnm1B is stabilized when bound to the telomere-binding protein TRF2.
    Freibaum BD, Counter CM., Free PMC Article

    01/21/2010
    Snm1B interacts with the Mre11-Rad50-Nbs1 (MRN) complex and with FancD2 further substantiating its role as a checkpoint/DNA repair protein.

    Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links.
    Bae JB, Mukhopadhyay SS, Liu L, Zhang N, Tan J, Akhter S, Liu X, Shen X, Li L, Legerski RJ., Free PMC Article

    01/21/2010
    siRNA knockdown of hSNM1B rendered cells sensitive to ionizing radiation, suggesting the possibility of hSNM1B involvement in homologous recombination repair of double-strand breaks arising as intermediates of ICL repair

    Human SNM1B is required for normal cellular response to both DNA interstrand crosslink-inducing agents and ionizing radiation.
    Demuth I, Digweed M, Concannon P.

    01/21/2010
    the C terminus of Snm1B was shown to interact with the TRF homology domain of TRF2 indicating that Snm1B is likely recruited to the telomere via interaction with the double-stranded telomere-binding protein TRF2

    hSnm1B is a novel telomere-associated protein.
    Freibaum BD, Counter CM.

    01/21/2010
    SNM1B (Apollo) is an Artemis-like nuclease that is required for the protection of telomeres during or after their replication. [Apollo]

    Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase.
    van Overbeek M, de Lange T.

    01/21/2010
    SNM1B (Apollo) protein exhibits a 5'-to-3' DNA exonuclease activity and functions together with TRF2 to protect telomeres from damage and fusion.

    The Apollo 5' exonuclease functions together with TRF2 to protect telomeres from DNA repair.
    Lenain C, Bauwens S, Amiard S, Brunori M, Giraud-Panis MJ, Gilson E.

    01/21/2010
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