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TRAPPC13 modulates autophagy and the response to Golgi stress.
Ramírez-Peinado S, Ignashkova TI, van Raam BJ, Baumann J, Sennott EL, Gendarme M, Lindemann RK, Starnbach MN, Reiling JH. Ramírez-Peinado S, et al. J Cell Sci. 2017 Jul 15;130(14):2251-2265. doi: 10.1242/jcs.199521. Epub 2017 May 23. J Cell Sci. 2017. PMID: 28536105 Free PMC article.
TRAPPC13 depletion reduces Rab1a and Rab1b activity, impairs autophagy and leads to increased infectivity to the pathogenic bacterium Shigella flexneri in response to brefeldin A. Thus, our results lend support for the existence of a mammalian TRAPPIII complex containing …
TRAPPC13 depletion reduces Rab1a and Rab1b activity, impairs autophagy and leads to increased infectivity to the pathogenic bacterium …
TRAPPC13 Is a Novel Target of Mesorhizobium amorphae Type III Secretion System Effector NopP.
Liu D, Luo Y, Zheng X, Wang X, Chou M, Wei G. Liu D, et al. Mol Plant Microbe Interact. 2021 May;34(5):511-523. doi: 10.1094/MPMI-12-20-0354-FI. Epub 2021 May 20. Mol Plant Microbe Interact. 2021. PMID: 33630651 Free article.
A trafficking protein particle complex subunit 13-like protein (TRAPPC13) has been identified as a NopP target protein in R. pseudoacacia roots by screening a yeast two-hybrid library. The physical interaction between NopP and TRAPPC13 is verified by bimolecular flu …
A trafficking protein particle complex subunit 13-like protein (TRAPPC13) has been identified as a NopP target protein in R. pseudoac …
Targeting of ASH Domain-Containing Proteins to the Centrosome.
Verdier P, Morthorst SK, Pedersen LB. Verdier P, et al. Methods Mol Biol. 2016;1454:15-33. doi: 10.1007/978-1-4939-3789-9_2. Methods Mol Biol. 2016. PMID: 27514913
By generating plasmids coding for epitope-tagged full-length (FL) or truncated versions of the ASH domain-containing proteins TRAPPC8, TRAPPC13, NPHP4, and DLEC1, followed by expression and quantitative immunofluorescence microscopy (IFM) analysis in cultured human telomer …
By generating plasmids coding for epitope-tagged full-length (FL) or truncated versions of the ASH domain-containing proteins TRAPPC8, TR …
Biochemical Insight into Novel Rab-GEF Activity of the Mammalian TRAPPIII Complex.
Harris NJ, Jenkins ML, Dalwadi U, Fleming KD, Nam SE, Parson MAH, Yip CK, Burke JE. Harris NJ, et al. J Mol Biol. 2021 Sep 3;433(18):167145. doi: 10.1016/j.jmb.2021.167145. Epub 2021 Jul 3. J Mol Biol. 2021. PMID: 34229011
These two complexes share a common core of subunits, with complex specific subunits (TRAPPC9 and TRAPPC10 in TRAPPII and TRAPPC8, TRAPPC11, TRAPPC12, TRAPPC13 in TRAPPIII). TRAPPII and TRAPPIII have distinct specificity for GEF activity towards Rabs, with TRAPPIII acting o …
These two complexes share a common core of subunits, with complex specific subunits (TRAPPC9 and TRAPPC10 in TRAPPII and TRAPPC8, TRAPPC11, …
Cryo-EM structure of metazoan TRAPPIII, the multi-subunit complex that activates the GTPase Rab1.
Galindo A, Planelles-Herrero VJ, Degliesposti G, Munro S. Galindo A, et al. EMBO J. 2021 Jun 15;40(12):e107608. doi: 10.15252/embj.2020107608. Epub 2021 May 21. EMBO J. 2021. PMID: 34018214 Free PMC article.
The TRAPPIII-specific subunits TRAPPC8 and TRAPPC11 hold the catalytic core like a pair of tongs, with TRAPPC12 and TRAPPC13 positioned at the joint between them. TRAPPC2 and TRAPPC2L link the core to the two large arms, with the interfaces containing residues affected by …
The TRAPPIII-specific subunits TRAPPC8 and TRAPPC11 hold the catalytic core like a pair of tongs, with TRAPPC12 and TRAPPC13 position …
The TRAPPIII complex regulates development and virulence of Fusarium graminearum by coordinating autophagy and intracellular transport.
Chen L, Zhang Y, Zhang G, Xu L, Ren M, Zhang L, Lu K, Chen X, Liang Y, Zou S, Dong H. Chen L, et al. PLoS Pathog. 2025 Oct 24;21(10):e1013627. doi: 10.1371/journal.ppat.1013627. eCollection 2025 Oct. PLoS Pathog. 2025. PMID: 41134853 Free PMC article.
Here, we identify four TRAPPIII-specific subunits (FgTrs85, TRAPPC11, TRAPPC12, and TRAPPC13) in the phytopathogenic fungus Fusarium graminearum. Genetic and functional analyses reveal that FgTrs85 serves as the core subunit, collaborating with auxiliary subunits TRAPPC11, …
Here, we identify four TRAPPIII-specific subunits (FgTrs85, TRAPPC11, TRAPPC12, and TRAPPC13) in the phytopathogenic fungus Fusarium …
Subclinical endometritis in dairy cattle is associated with distinct mRNA expression patterns in blood and endometrium.
Raliou M, Dembélé D, Düvel A, Bolifraud P, Aubert J, Mary-Huard T, Rocha D, Piumi F, Mockly S, Heppelmann M, Dieuzy-Labaye I, Zieger P, G E Smith D, Schuberth HJ, Sheldon IM, Sandra O. Raliou M, et al. PLoS One. 2019 Aug 2;14(8):e0220244. doi: 10.1371/journal.pone.0220244. eCollection 2019. PLoS One. 2019. PMID: 31374089 Free PMC article.
Among these genes, transcript abundance of immune factors C3, C2, LTF, PF4 and TRAPPC13 were up-regulated in SCE cows at 45-55 days postpartum. Moreover, mRNA expression of C3, CXCL8, LTF, TLR2 and TRAPPC13 was temporally regulated during the postpartum period in ci …
Among these genes, transcript abundance of immune factors C3, C2, LTF, PF4 and TRAPPC13 were up-regulated in SCE cows at 45-55 days p …
Characterization of Aspergillus nidulans TRAPPs uncovers unprecedented similarities between fungi and metazoans and reveals the modular assembly of TRAPPII.
Pinar M, Arias-Palomo E, de Los Ríos V, Arst HN Jr, Peñalva MA. Pinar M, et al. PLoS Genet. 2019 Dec 23;15(12):e1008557. doi: 10.1371/journal.pgen.1008557. eCollection 2019 Dec. PLoS Genet. 2019. PMID: 31869332 Free PMC article.
We show that Aspergillus TRAPPIII contains homologues of metazoan TRAPPC11, TRAPPC12 and TRAPPC13 subunits, absent in S. cerevisiae, and establish that these subunits are recruited to the complex by Tca17/TRAPPC2L, which itself binds to the 'Trs33 side' of the complex. ...
We show that Aspergillus TRAPPIII contains homologues of metazoan TRAPPC11, TRAPPC12 and TRAPPC13 subunits, absent in S. cerevisiae, …