TRAPPC8

Last update 08 May 2025

Basic Info

Synonyms

GSG1, HsT2706, KIAA1012

+ [4]

Introduction

Plays a role in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage (PubMed:21525244). Maintains together with TBC1D14 the cycling pool of ATG9 required for initiation of autophagy (PubMed:26711178). Involved in collagen secretion (PubMed:32095531).

100 Clinical Results associated with TRAPPC8

100 Translational Medicine associated with TRAPPC8

0 Patents (Medical) associated with TRAPPC8

Literatures (Medical) associated with TRAPPC8

01 Mar 2025·Plant Physiology

The TRAPPC8/TRS85 subunit of the Arabidopsis TRAPPIII tethering complex regulates endoplasmic reticulum function and autophagy

Article

Author: Nowakowska, Julita ; Piłka, Natalia ; Swiezewska, Ewa ; Hoffman-Sommer, Marta ; Pączkowski, Cezary ; Kozieradzka-Kiszkurno, Małgorzata ; Steczkiewicz, Kamil ; Dagdas, Yasin ; Jemioła-Rzemińska, Małgorzata ; Anielska-Mazur, Anna

AbstractTransport protein particle (TRAPP) tethering complexes are known for their function as Rab GTPase exchange factors. Two versions of the complex are considered functionally separate: TRAPPII, an activator of the Rab11 family (RabA in plants) GTPases that function in post-Golgi sorting, and TRAPPIII, activating Rab1 family (RabD in plants) members that regulate endoplasmic reticulum (ER)-to-Golgi trafficking and autophagy. In Arabidopsis (Arabidopsis thaliana), the TRAPPIII complex has been identified and its subunit composition established, but little is known about its functions. 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 in plants, we characterized 2 A. thaliana trappc8 mutants. These mutants display abnormalities in plant morphology, particularly in flower and seed development. They also exhibit autophagic defects, a constitutive ER stress response, and elevated levels of the ER lipid dolichol (Dol), which is an indispensable cofactor in protein glycosylation. These results indicate that plant TRAPPC8 is involved in multiple cellular trafficking events and suggest a link between ER stress responses and Dol levels.

01 Jun 2024·The Plant Journal

The TRAPPIII subunit, Trs85, has a dual role in the trafficking of cellulose synthase complexes in Arabidopsis

Article

Author: Allen, Holly ; Li, Shundai ; Gu, Ying ; Zhu, Xiaoyu

SUMMARYPlant cell walls are essential for defining plant growth and development, providing structural support to the main body and responding to abiotic and biotic cues. Cellulose, the main structural polymer of plant cell walls, is synthesized at the plasma membrane by cellulose synthase complexes (CSCs). The construction and transport of CSCs to and from the plasma membrane is poorly understood but is known to rely on the coordinated activity of cellulose synthase‐interactive protein 1 (CSI1), a key regulator of CSC trafficking. In this study, we found that Trs85, a TRAPPIII complex subunit, interacted with CSI1 in vitro. Using functional genetics and live‐cell imaging, we have shown that trs85‐1 mutants have reduced cellulose content, stimulated CSC delivery, an increased population of static CSCs and deficient clathrin‐mediated endocytosis in the primary cell wall. Overall, our findings suggest that Trs85 has a dual role in the trafficking of CSCs, by negatively regulating the exocytosis and clathrin‐mediated endocytosis of CSCs.

01 Feb 2024·Plant Communications

SP-141 targets Trs85 to inhibit rice blast fungus infection and functions as a potential broad-spectrum antifungal agent

Article

Author: Li, Lin ; Yu, Bin ; Wang, Ying ; Lin, Fu-Cheng ; Bao, Jian-Dong ; Cheng, Jing-Li ; Wu, Xi-Yu ; Liu, Xiao-Hong ; Xu, Fei ; Cai, Ying-Ying ; Lu, Jian-Ping ; Dong, Bo ; Zhu, Xue-Ming

Rice blast is a devastating disease worldwide, threatening rice production and food security. The blast fungus Magnaporthe oryzae invades the host via the appressorium, a specialized pressure-generating structure that generates enormous turgor pressure to penetrate the host cuticle. However, owing to ongoing evolution of fungicide resistance, it is vitally important to identify new targets and fungicides. Here, we show that Trs85, a subunit of the transport protein particle III complex, is essential for appressorium-mediated infection in M. oryzae. We explain how Trs85 regulates autophagy through Ypt1 (a small guanosine triphosphatase protein) in M. oryzae. We then identify a key conserved amphipathic α helix within Trs85 that is associated with pathogenicity of M. oryzae. Through computer-aided screening, we identify a lead compound, SP-141, that affects autophagy and the Trs85-Ypt1 interaction. SP-141 demonstrates a substantial capacity to effectively inhibit infection caused by the rice blast fungus while also exhibiting wide-ranging potential as an antifungal agent with broad-spectrum activity. Taken together, our data show that Trs85 is a potential new target and that SP-141 has potential for the control of rice blast. Our findings thus provide a novel strategy that may help in the fight against rice blast.

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TRAPPC8

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