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    Sppl2a signal peptide peptidase like 2A [ Mus musculus (house mouse) ]

    Gene ID: 66552, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The intramembrane proteases SPPL2a and SPPL2b regulate the homeostasis of selected SNARE proteins.

    The intramembrane proteases SPPL2a and SPPL2b regulate the homeostasis of selected SNARE proteins.
    Ballin M, Griep W, Patel M, Karl M, Mentrup T, Rivera-Monroy J, Foo B, Schwappach B, Schröder B.

    05/7/2023
    Deficiency of the Intramembrane Protease SPPL2a Alters Antimycobacterial Cytokine Responses of Dendritic Cells.

    Deficiency of the Intramembrane Protease SPPL2a Alters Antimycobacterial Cytokine Responses of Dendritic Cells.
    Gradtke AC, Mentrup T, Lehmann CHK, Cabrera-Cabrera F, Desel C, Okakpu D, Assmann M, Dalpke A, Schaible UE, Dudziak D, Schröder B.

    05/22/2021
    SPPL2a/b negatively regulates LOX-1 signaling and atherosclerosis.

    Atherogenic LOX-1 signaling is controlled by SPPL2-mediated intramembrane proteolysis.
    Mentrup T, Theodorou K, Cabrera-Cabrera F, Helbig AO, Happ K, Gijbels M, Gradtke AC, Rabe B, Fukumori A, Steiner H, Tholey A, Fluhrer R, Donners M, Schröder B., Free PMC Article

    05/9/2020
    Sppl2a-/- mice lack conventional dendritic cells, have CD4+ T cells that produce small amounts of IFN-gamma after BCG infection, and are highly susceptible to infection with BCG or Mycobacterium tuberculosis

    Disruption of an antimycobacterial circuit between dendritic and helper T cells in human SPPL2a deficiency.
    Kong XF, Martinez-Barricarte R, Kennedy J, Mele F, Lazarov T, Deenick EK, Ma CS, Breton G, Lucero KB, Langlais D, Bousfiha A, Aytekin C, Markle J, Trouillet C, Jabot-Hanin F, Arlehamn CSL, Rao G, Picard C, Lasseau T, Latorre D, Hambleton S, Deswarte C, Itan Y, Abarca K, Moraes-Vasconcelos D, Ailal F, Ikinciogullari A, Dogu F, Benhsaien I, Sette A, Abel L, Boisson-Dupuis S, Schröder B, Nussenzweig MC, Liu K, Geissmann F, Tangye SG, Gros P, Sallusto F, Bustamante J, Casanova JL., Free PMC Article

    05/25/2019
    Study propose that elements within the transmembrane segment and the luminal juxtamembrane domain facilitate intramembrane proteolysis of CD74 by SPPL2a.

    Substrate determinants of signal peptide peptidase-like 2a (SPPL2a)-mediated intramembrane proteolysis of the invariant chain CD74.
    Hüttl S, Helfrich F, Mentrup T, Held S, Fukumori A, Steiner H, Saftig P, Fluhrer R, Schröder B.

    05/20/2017
    SPPL2a-mediated processing of CD74 NTF is indispensable to maintain appropriate levels of tonic BCR signaling to promote B cell maturation.

    Processing of CD74 by the Intramembrane Protease SPPL2a Is Critical for B Cell Receptor Signaling in Transitional B Cells.
    Hüttl S, Kläsener K, Schweizer M, Schneppenheim J, Oberg HH, Kabelitz D, Reth M, Saftig P, Schröder B.

    11/28/2015
    Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).

    Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).
    Brady OA, Zhou X, Hu F., Free PMC Article

    10/4/2014
    in vivo SPPL2a, but not SPPL2b, exhibit a physiologically relevant contribution to CD74 proteolysis in B and dendritic cells

    The intramembrane proteases signal Peptide peptidase-like 2a and 2b have distinct functions in vivo.
    Schneppenheim J, Hüttl S, Mentrup T, Lüllmann-Rauch R, Rothaug M, Engelke M, Dittmann K, Dressel R, Araki M, Araki K, Wienands J, Fluhrer R, Saftig P, Schröder B., Free PMC Article

    05/24/2014
    intramembrane proteolysis by SPPL2A is essential for maintaining cellular homeostasis of ameloblasts.

    The intramembrane protease SPPL2A is critical for tooth enamel formation.
    Bronckers AL, Gueneli N, Lüllmann-Rauch R, Schneppenheim J, Moraru AP, Himmerkus N, Bervoets TJ, Fluhrer R, Everts V, Saftig P, Schröder B.

    11/16/2013
    B cell survival and dendritic cells function requires SPPL2A.

    B cell survival, surface BCR and BAFFR expression, CD74 metabolism, and CD8- dendritic cells require the intramembrane endopeptidase SPPL2A.
    Bergmann H, Yabas M, Short A, Miosge L, Barthel N, Teh CE, Roots CM, Bull KR, Jeelall Y, Horikawa K, Whittle B, Balakishnan B, Sjollema G, Bertram EM, Mackay F, Rimmer AJ, Cornall RJ, Field MA, Andrews TD, Goodnow CC, Enders A., Free PMC Article

    04/13/2013
    Sppl2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain.

    The intramembrane protease SPPL2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain.
    Schneppenheim J, Dressel R, Hüttl S, Lüllmann-Rauch R, Engelke M, Dittmann K, Wienands J, Eskelinen EL, Hermans-Borgmeyer I, Fluhrer R, Saftig P, Schröder B., Free PMC Article

    04/13/2013
    Sppl2a is required for B cell and dendritic cells development and survival.

    The intramembrane protease Sppl2a is required for B cell and DC development and survival via cleavage of the invariant chain.
    Beisner DR, Langerak P, Parker AE, Dahlberg C, Otero FJ, Sutton SE, Poirot L, Barnes W, Young MA, Niessen S, Wiltshire T, Bodendorf U, Martoglio B, Cravatt B, Cooke MP., Free PMC Article

    04/13/2013
    Data show that endogenous SPPL2a - in agreement with overexpression studies - is localised in membranes of lysosomes/late endosomes.

    Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail.
    Behnke J, Schneppenheim J, Koch-Nolte F, Haag F, Saftig P, Schröder B.

    12/31/2011
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