MAP kinase-activating death domain protein

Definition:

Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family. Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms. Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2. May link TNFRSF1A with MAP kinase activation. May be involved in the regulation of TNFA-induced apoptosis.

References:

[1]. Shin-ichiro Yoshimura, et al. Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors. J Cell Biol. 2010 Oct 18;191(2):367-81. [Content Brief]

[2]. Ana C Figueiredo, et al. Rab3GEP is the non-redundant guanine nucleotide exchange factor for Rab27a in melanocytes. J Biol Chem. 2008 Aug 22;283(34):23209-16. [Content Brief]

[3]. Pauline E Schneeberger, et al. Biallelic MADD variants cause a phenotypic spectrum ranging from developmental delay to a multisystem disorder. Brain. 2020 Aug 1;143(8):2437-2453. [Content Brief]

[4]. A R Schievella, et al. MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase. J Biol Chem. 1997 May 2;272(18):12069-75. [Content Brief]

[5]. A M Al-Zoubi, et al. Contrasting effects of IG20 and its splice isoforms, MADD and DENN-SV, on tumor necrosis factor alpha-induced apoptosis and activation of caspase-8 and -3. J Biol Chem. 2001 Dec 14;276(50):47202-11. [Content Brief]

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