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    Cadps calcium dependent secretion activator [ Rattus norvegicus (Norway rat) ]

    Gene ID: 26989, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Down-regulation of habenular calcium-dependent secretion activator 2 induces despair-like behavior.

    Down-regulation of habenular calcium-dependent secretion activator 2 induces despair-like behavior.
    Yoo H, Yang SH, Kim JY, Yang E, Park HS, Lee SJ, Rhyu IJ, Turecki G, Lee HW, Kim H., Free PMC Article

    12/18/2021
    The unique tandem C2-PH domain of CAPS may serve as a PI(4,5)P2-triggered switch for dimerization. CAPS dimerization may be coupled to oligomeric SNARE complex assembly for vesicle docking and priming.

    The Vesicle Priming Factor CAPS Functions as a Homodimer via C2 Domain Interactions to Promote Regulated Vesicle Exocytosis.
    Petrie M, Esquibel J, Kabachinski G, Maciuba S, Takahashi H, Edwardson JM, Martin TF., Free PMC Article

    05/20/2017
    results indicate that dense-core vesicles carry CAPS to sites of exocytosis, where CAPS promotes vesicle docking and fusion competence, probably by initiating SNARE complex assembly.

    Resident CAPS on dense-core vesicles docks and primes vesicles for fusion.
    Kabachinski G, Kielar-Grevstad DM, Zhang X, James DJ, Martin TF., Free PMC Article

    09/24/2016
    Transport vesicle fusion into PIP2-rich membrane domains is facilitated by sequential PIP2-dependent activation of CAPS and PIP2-dependent recruitment of Munc13.

    CAPS and Munc13 utilize distinct PIP2-linked mechanisms to promote vesicle exocytosis.
    Kabachinski G, Yamaga M, Kielar-Grevstad DM, Bruinsma S, Martin TF., Free PMC Article

    01/17/2015
    CAPS1 binds to the full-length of cytoplasmic syntaxin-1 with preference to its "open" conformation, whereas Munc13-1 binds to the first 80 N-terminal residues of syntaxin-1.

    Calcium-dependent activator protein for secretion 1 (CAPS1) binds to syntaxin-1 in a distinct mode from Munc13-1.
    Parsaud L, Li L, Jung CH, Park S, Saw NM, Park S, Kim MY, Sugita S., Free PMC Article

    11/2/2013
    The results show that Munc13 homology domain-1 is a SNARE-binding domain and that SNARE protein binding is essential for CAPS function in dense-core vesicle exocytosis.

    Munc13 homology domain-1 in CAPS/UNC31 mediates SNARE binding required for priming vesicle exocytosis.
    Khodthong C, Kabachinski G, James DJ, Martin TF., Free PMC Article

    01/7/2012
    Results suggest that SNARE complex formation promoted by CAPS may be mediated by direct interactions of CAPS with each of the three SNARE proteins required.

    Novel interactions of CAPS (Ca2+-dependent activator protein for secretion) with the three neuronal SNARE proteins required for vesicle fusion.
    Daily NJ, Boswell KL, James DJ, Martin TF., Free PMC Article

    02/26/2011
    a functional role for CAPS1 in regulating DCV trafficking in the trans-Golgi network; this activity occurs via protein-protein interaction with ARF4/ARF5 in a GDP-dependent manner.

    Interaction of calcium-dependent activator protein for secretion 1 (CAPS1) with the class II ADP-ribosylation factor small GTPases is required for dense-core vesicle trafficking in the trans-Golgi network.
    Sadakata T, Shinoda Y, Sekine Y, Saruta C, Itakura M, Takahashi M, Furuichi T., Free PMC Article

    01/1/2011
    Data suggest that CAPS functions in priming vesicle exocytosis by coupling membrane binding to SNARE complexes. assembly.

    Phosphatidylinositol 4,5-bisphosphate regulation of SNARE function in membrane fusion mediated by CAPS.
    James DJ, Khodthong C, Kowalchyk JA, Martin TF., Free PMC Article

    08/9/2010
    CAPS activity in priming vesicle exocytosis requires CK2 phosphorylation

    CAPS activity in priming vesicle exocytosis requires CK2 phosphorylation.
    Nojiri M, Loyet KM, Klenchin VA, Kabachinski G, Martin TF., Free PMC Article

    01/21/2010
    CAPS proteins are involved in optimizing vesicular monoamine uptake and storage mediated by VMAT1 and VMAT2

    Ca2+-dependent activator proteins of secretion promote vesicular monoamine uptake.
    Brunk I, Blex C, Speidel D, Brose N, Ahnert-Hilger G.

    01/21/2010
    CAPS1 has a role in constitutive and regulated exocytosis but not in loading of transmitters into dense core vesicles

    Ca2+-dependent activator protein for secretion 1 is critical for constitutive and regulated exocytosis but not for loading of transmitters into dense core vesicles.
    Fujita Y, Xu A, Xie L, Arunachalam L, Chou TC, Jiang T, Chiew SK, Kourtesis J, Wang L, Gaisano HY, Sugita S.

    01/21/2010
    The three variants CaM mutants were able to activate the cyclic nucleotide phosphodiesterase and the plasma membrane Ca(2+)-ATPase,and present the characteristic Ca(2+)-induced electrophoretic mobility shift of native CaM.

    Characterisation of tyrosine-phosphorylation-defective calmodulin mutants.
    Salas V, Sánchez-Torres J, Cusidó-Hita DM, García-Marchan Y, Sojo F, Benaim G, Villalobo A.

    01/21/2010
    CAPS-1 functions following ATP-dependent priming as a phosphatidylinositol 4,5-diphosphate binding protein to enhance Ca2+-dependent exocytosis of dense-core vesicles.

    CAPS acts at a prefusion step in dense-core vesicle exocytosis as a PIP2 binding protein.
    Grishanin RN, Kowalchyk JA, Klenchin VA, Ann K, Earles CA, Chapman ER, Gerona RR, Martin TF.

    01/21/2010
    CAPS plays a role in the regulated exocytosis of calcium-triggered dense-core vesicles in the nervous and endocrine systems

    Role of CAPS in dense-core vesicle exocytosis.
    Wassenberg JJ, Martin TF.

    01/21/2010
    Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS).

    Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS).
    Binda AV, Kabbani N, Levenson R.

    01/21/2010
    identification, cloning, and comparative characterization of a second mammalian CAPS isoform, CAPS2; concluded that at the functional level, CAPS2 is largely redundant with CAPS1.

    A family of Ca2+-dependent activator proteins for secretion: comparative analysis of structure, expression, localization, and function.
    Speidel D, Varoqueaux F, Enk C, Nojiri M, Grishanin RN, Martin TF, Hofmann K, Brose N, Reim K.

    01/21/2010
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