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The TRAPPC8/TRS85 subunit of the Arabidopsis TRAPPIII tethering complex regulates endoplasmic reticulum function and autophagy.
Hoffman-Sommer M, Piłka N, Anielska-Mazur A, Nowakowska J, Kozieradzka-Kiszkurno M, Pączkowski C, Jemioła-Rzemińska M, Steczkiewicz K, Dagdas Y, Swiezewska E. Hoffman-Sommer M, et al. Plant Physiol. 2025 Mar 1;197(3):kiaf042. doi: 10.1093/plphys/kiaf042. Plant Physiol. 2025. PMID: 40084709 Free PMC article.
Here, we found that binary subunit interactions of the plant TRAPPIII complex are analogous to those of metazoan TRAPPIII, with the 2 large subunits TRAPPC8 and TRAPPC11 linking the TRAPP core and the small C12 to C13 dimer. To gain insight into the functions of TRAPPIII i …
Here, we found that binary subunit interactions of the plant TRAPPIII complex are analogous to those of metazoan TRAPPIII, with the 2 large …
Distinct Roles of TRAPPC8 and TRAPPC12 in Ciliogenesis via Their Interactions With OFD1.
Zhang C, Li C, Siu GKY, Luo X, Yu S. Zhang C, et al. Front Cell Dev Biol. 2020 Mar 17;8:148. doi: 10.3389/fcell.2020.00148. eCollection 2020. Front Cell Dev Biol. 2020. PMID: 32258032 Free PMC article.
We found a ciliopathy protein, oral-facial-digital syndrome 1 (OFD1), interacting with the TRAPPIII-specific subunits TRAPPC8 and TRAPPC12. TRAPPC8 is necessary for the association of OFD1 with pericentriolar material 1 (PCM1). ...Overall, this study has revealed di …
We found a ciliopathy protein, oral-facial-digital syndrome 1 (OFD1), interacting with the TRAPPIII-specific subunits TRAPPC8 and TRA …
Identification of TRAPPC8 as a host factor required for human papillomavirus cell entry.
Ishii Y, Nakahara T, Kataoka M, Kusumoto-Matsuo R, Mori S, Takeuchi T, Kukimoto I. Ishii Y, et al. PLoS One. 2013 Nov 14;8(11):e80297. doi: 10.1371/journal.pone.0080297. eCollection 2013. PLoS One. 2013. PMID: 24244674 Free PMC article.
TRAPPC8 knockdown in HaCaT cells also showed reduced susceptibility to infection with authentic HPV31 virions, indicating that TRAPPC8 plays a crucial role in native HPV infection. ...Finally, expression of GFP-fused L2 that can also interact with TRAPPC8 ind
TRAPPC8 knockdown in HaCaT cells also showed reduced susceptibility to infection with authentic HPV31 virions, indicating that TRA
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.
We report a cryo-EM structure of the entire Drosophila TRAPPIII complex. 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 …
We report a cryo-EM structure of the entire Drosophila TRAPPIII complex. The TRAPPIII-specific subunits TRAPPC8 and TRAPPC11 hold the …
The adaptor function of TRAPPC2 in mammalian TRAPPs explains TRAPPC2-associated SEDT and TRAPPC9-associated congenital intellectual disability.
Zong M, Wu XG, Chan CW, Choi MY, Chan HC, Tanner JA, Yu S. Zong M, et al. PLoS One. 2011;6(8):e23350. doi: 10.1371/journal.pone.0023350. Epub 2011 Aug 15. PLoS One. 2011. PMID: 21858081 Free PMC article.
Unexpectedly, TRAPPC2 can also bind to the putative TRAPPIII-specific subunit, TRAPPC8. Endogenous TRAPPC9-positive TRAPPII complex does not contain TRAPPC8, suggesting that TRAPPC2 binds to either TRAPPC9 or TRAPPC8 during the formation of the mammalian equi …
Unexpectedly, TRAPPC2 can also bind to the putative TRAPPIII-specific subunit, TRAPPC8. Endogenous TRAPPC9-positive TRAPPII complex d …
Identification of conserved, centrosome-targeting ASH domains in TRAPPII complex subunits and TRAPPC8.
Schou KB, Morthorst SK, Christensen ST, Pedersen LB. Schou KB, et al. Cilia. 2014 Jun 18;3:6. doi: 10.1186/2046-2530-3-6. eCollection 2014. Cilia. 2014. PMID: 25018876 Free PMC article.
We identified the TRAPP complex subunits TRAPPC8, -9, -10, -11, and -13 as novel ASH domain-containing proteins. In addition to a C-terminal ASH domain region, we predict that the N-terminus of TRAPPC8, -9, -10, and -11, as well as their yeast counterparts, consists …
We identified the TRAPP complex subunits TRAPPC8, -9, -10, -11, and -13 as novel ASH domain-containing proteins. In addition to a C-t …
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
TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic.
Lamb CA, Nühlen S, Judith D, Frith D, Snijders AP, Behrends C, Tooze SA. Lamb CA, et al. EMBO J. 2016 Feb 1;35(3):281-301. doi: 10.15252/embj.201592695. Epub 2015 Dec 28. EMBO J. 2016. PMID: 26711178 Free PMC article.
TBC1D14 binds to the TRAPP complex via an N-terminal 103 amino acid region, and overexpression of this region inhibits both autophagy and secretory traffic. TRAPPC8, the mammalian orthologue of a yeast autophagy-specific TRAPP subunit, forms part of a mammalian TRAPPIII-li …
TBC1D14 binds to the TRAPP complex via an N-terminal 103 amino acid region, and overexpression of this region inhibits both autophagy and se …
Atg9A trafficking through the recycling endosomes is required for autophagosome formation.
Imai K, Hao F, Fujita N, Tsuji Y, Oe Y, Araki Y, Hamasaki M, Noda T, Yoshimori T. Imai K, et al. J Cell Sci. 2016 Oct 15;129(20):3781-3791. doi: 10.1242/jcs.196196. Epub 2016 Sep 1. J Cell Sci. 2016. PMID: 27587839
The combination of defects in autophagy and Atg9A accumulation in the recycling endosomes was also found upon the knockdown of TRAPPC8, a specific subunit of the TRAPPIII complex. These results show directly that the trafficking of Atg9A through the recycling endosomes is …
The combination of defects in autophagy and Atg9A accumulation in the recycling endosomes was also found upon the knockdown of TRAPPC8
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, TRA …
16 results