Revealing Functional Crosstalk between Distinct Bioprocesses through Reciprocal Functional Tests of Genetically Interacting Genes

Chen, Dan; Xu, Wei; Wang, Yu; Ye, Yongshen; Wang, Yue; Yu, Miao; Gao, Jinghu; Wei, Jiaolong; Dong, Yun; Zhang, Honghua; Fu, Xin; Ma, Ke; Wang, Hui; Yang, Zihao; Zhou, Jie; Cheng, Wenqing; Shu, Wang; Chen, Juan; Grant, Barth D.; Myers, Chad L.; Shi, Anbing; Xia, Tian

doi:10.1016/j.celrep.2019.10.076

Cited by 2 publications

(3 citation statements)

References 70 publications

(112 reference statements)

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“…However, the mechanism controlling the localization of SMAPs is still not well understood. Here, by using a well-established in vivo membrane trafficking investigation model ( Chen et al, 2018 ; Chen et al, 2019 ; Gao et al, 2020 ; Zhang et al, 2020 ; Yan et al, 2021 ), we showed that the integrity of AP-1 adaptor is necessary for the TGN positioning of SMAP-1. Although we did not specifically identify which AP-1 subunit governs the TGN localization of SMAP-1, our results suggested that in addition to CALM, SMAP-1 underlies an additional clathrin assembly mechanism, enriching the understanding of AP-1/clathrin coat assembly.…”

Section: Discussionmentioning

confidence: 89%

AP-1 Recruits SMAP-1/SMAPs to the trans-Golgi Network to Promote Sorting in Polarized Epithelia

Wang

Yao

Zhang

et al. 2021

Front. Cell Dev. Biol.

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Coordinated AP-1 and clathrin coat assembly mediate secretory sorting on the trans-Golgi network (TGN) during conventional secretion. Here we found that SMAP-1/SMAPs deficiency caused the apical protein ERM-1 to accumulate on the basolateral side of the TGN. In contrast, the basolateral protein SLCF-1 appeared abnormally on the apical membrane. SMAP-1 colocalized with AP-1 on the TGN. The integrity of AP-1 is required for the subcellular presence of SMAP-1. Moreover, we found that the loss of SMAP-1 reduced clathrin-positive structures in the cytosol, suggesting that SMAP-1 has a regulatory role in clathrin assembly on the TGN. Functional experiments showed that overexpressing clathrin effectively alleviated exocytic defects due to the lack of SMAP-1, corroborating the role of SMAP-1 in promoting the assembly of clathrin on the TGN. Together, our results suggested that the AP-1 complex regulates the TGN localization of SMAP-1, promoting clathrin assembly to ensure polarized conventional secretion in C. elegans intestinal epithelia.

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Section: Discussionmentioning

confidence: 89%

AP-1 Recruits SMAP-1/SMAPs to the trans-Golgi Network to Promote Sorting in Polarized Epithelia

Wang

Yao

Zhang

et al. 2021

Front. Cell Dev. Biol.

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“…Cdc42, a Rho GTPase involved in the regulation of cell cycle, has been reported to modulate the bidirectional transport of COPI vesicles at the Golgi 8 . In addition, an inter‐bioprocess genetic interaction analysis revealed functional connections between intracellular transport and other bioprocesses such as aging 9 . Currently, the regulation of the folding process and homeostasis of many trafficking proteins remains largely unclear.…”

Section: Introductionmentioning

confidence: 99%

“…8 In addition, an inter-bioprocess genetic interaction analysis revealed functional connections between intracellular transport and other bioprocesses such as aging. 9 Currently, the regulation of the folding process and homeostasis of many trafficking proteins remains largely unclear.…”

Section: Introductionmentioning

confidence: 99%

A genome‐wide CRISPR screen identifies the CCT chaperonin as a critical regulator of vesicle trafficking

et al. 2023

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Vesicle trafficking is a fundamental cellular process that controls the transport of various proteins and cargos between cellular compartments in eukaryotes. Using a combination of genome‐wide CRISPR screening in mammalian cells and RNAi screening in Caenorhabditis elegans, we identify chaperonin containing TCP‐1 subunit 4 (CCT4) as a critical regulator of protein secretion and vesicle trafficking. In C. elegans, deficiency of cct‐4 as well as other CCT subunits impairs the trafficking of endocytic markers in intestinal cells, and this defect resembles that of dyn‐1 RNAi worms. Consistent with these findings, the silencing of CCT4 in human cells leads to defective endosomal trafficking, and this defect can be rescued by the dynamin activator Ryngo 1–23. These results suggest that the cytosolic chaperonin CCT may regulate vesicle trafficking by promoting the folding of dynamin in addition to its known substrate tubulin. Our findings establish an essential role for the CCT chaperonin in regulating vesicle trafficking, and provide new insights into the regulation of vesicle trafficking and the cellular function of the cytosolic chaperonin.

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Revealing Functional Crosstalk between Distinct Bioprocesses through Reciprocal Functional Tests of Genetically Interacting Genes

Cited by 2 publications

References 70 publications

AP-1 Recruits SMAP-1/SMAPs to the trans-Golgi Network to Promote Sorting in Polarized Epithelia

AP-1 Recruits SMAP-1/SMAPs to the trans-Golgi Network to Promote Sorting in Polarized Epithelia

A genome‐wide CRISPR screen identifies the CCT chaperonin as a critical regulator of vesicle trafficking

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