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    APLP2 amyloid beta precursor like protein 2 [ Homo sapiens (human) ]

    Gene ID: 334, updated on 3-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    YWK-II (APLP2 protein) is a G(o)-coupled receptor for Mullerian inhibiting substance in mediating ERK1/2 activation leading to anti-apoptotic activity or cell survival.

    YWK-II protein as a novel G(o)-coupled receptor for Müllerian inhibiting substance in cell survival.
    Yin X, Ouyang S, Xu W, Zhang X, Fok KL, Wong HY, Zhang J, Qiu X, Miao S, Chan HC, Wang L.

    01/21/2010
    findings show an increase in the immunoreactivities for the nuclear C-terminal fragments of APLP2 and for GSK-3beta in the brains of Alzheimer disease patients

    Intracellular domains of amyloid precursor-like protein 2 interact with CP2 transcription factor in the nucleus and induce glycogen synthase kinase-3beta expression.
    Xu Y, Kim HS, Joo Y, Choi Y, Chang KA, Park CH, Shin KY, Kim S, Cheon YH, Baik TK, Kim JH, Suh YH.

    01/21/2010
    APLP2 and APP have roles in sperm function

    Differential distribution of Alzheimer's amyloid precursor protein family variants in human sperm.
    Fardilha M, Vieira SI, Barros A, Sousa M, Da Cruz e Silva OA, Da Cruz e Silva EF.

    01/21/2010
    APLP2 is shed by disintegrins and metalloproteinases. Overexpression of secretase or TACE in HEK293 cells increases the release of neurotrophic soluble APLP2 severalfold.

    Shedding of the amyloid precursor protein-like protein APLP2 by disintegrin-metalloproteinases.
    Endres K, Postina R, Schroeder A, Mueller U, Fahrenholz F.

    01/21/2010
    APLP1 and APLP2 are processed by the gamma-secretase in a Presenilin 1-dependent manner and the extreme carboxyl-terminal fragments produced by this processing (APP-like Intracellular Domain are able to enhance Fe65-dependent gene activation

    Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription.
    Scheinfeld MH, Ghersi E, Laky K, Fowlkes BJ, D'Adamio L.

    01/21/2010
    Sustained levels of APP and the elevated levels of APLP2, in spite of the reduced mRNA expression, are due to altered proteolytic processing of these proteins.

    Accumulation of the amyloid precursor-like protein APLP2 and reduction of APLP1 in retinoic acid-differentiated human neuroblastoma cells upon curcumin-induced neurite retraction.
    Adlerz L, Beckman M, Holback S, Tehranian R, Cortés Toro V, Iverfeldt K.

    01/21/2010
    APLP1 and APLP2 and APP are processed similarly to act via the same nuclear target and are regulated by BACE 1 in neurons

    Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1.
    Li Q, Südhof TC.

    01/21/2010
    APLP-1 and APLP-2 are processed by alpha- and gamma-secretase-like cleavages, and their intracellular domains can be released by cleavage at epsilon-sites. APLP-2 processing appears to be the most elaborate and to involve alternative cleavage sites.

    The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation.
    Eggert S, Paliga K, Soba P, Evin G, Masters CL, Weidemann A, Beyreuther K.

    01/21/2010
    The APLP2 gene has no CAGA box, but it does have a GAGA sequence in a location similar to that of the CAGA box in the APP gene.

    Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease.
    Maloney B, Ge YW, Greig N, Lahiri DK.

    01/21/2010
    Interaction of human and murine Abeta peptides, Abeta40 and Abeta42. Interspecies Abeta aggregates and fibres are readily formed and are more stable than homogenous human fibres. (Amyloid beta 40 and 42)

    Interaction of human and mouse Abeta peptides.
    Fung J, Frost D, Chakrabartty A, McLaurin J.

    01/21/2010
    crystals of extracellular fragment X3 of a human sperm membrane protein YWK-II/APPH have been grow by the vapour-diffusion method [YWK-II PROTEIN]

    Crystallization and preliminary crystallographic analysis of extracellular fragment X3 of YWK-II/APPH: a human sperm membrane protein related to the Alzheimer betaA4-amyloid precursor protein.
    Yang M, Zhou W, Zhang X, Hu W, Gao F, Pang H, Miao S, Wang L, Rao Z.

    01/21/2010
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