TRAPPC2L is a Novel, Highly Conserved TRAPP‐Interacting Protein

Scrivens, P. James; Shahrzad, Nassim; Moores, Adrian; Morin, Audrey; Brunet, Stephanie; Sacher, Michael

doi:10.1111/j.1600-0854.2009.00906.x

Cited by 49 publications

(82 citation statements)

References 51 publications

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“…In contrast, we now show that TRAPPC2L interacts with TRAPPC10 and identify Asp37 as a residue that is critical for this interaction. This residue is one of only two invariant amino acids detected as revealed by a multiple sequence alignment between TRAPPC2 and TRAPPC2L,22 suggesting that they may perform a similar function. While the equivalent missense variant in TRAPPC2 (p.Asp47Tyr) results in SEDT,44 the missense variant in TRAPPC2L does not as seen in both S1 and S2 in this study.…”

Section: Discussionmentioning

confidence: 93%

Bi-allelic mutations in TRAPPC2L result in a neurodevelopmental disorder and have an impact on RAB11 in fibroblasts

et al. 2018

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Section: Discussionmentioning

confidence: 93%

Bi-allelic mutations in TRAPPC2L result in a neurodevelopmental disorder and have an impact on RAB11 in fibroblasts

et al. 2018

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“…All other cargoes examined exited the ER and reached the plasma membrane at apparently normal rates. Sedlin plays its role in PC trafficking as a TRAPP component, because a similar selective impairment of the ER exit of PC was induced by depleting the whole TRAPP by knockdown of Bet3 (TRAPPC3), a core component of the complex that, when depleted, destabilizes TRAPP (12) (fig. S1A and figs.…”

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confidence: 99%

Sedlin Controls the ER Export of Procollagen by Regulating the Sar1 Cycle

Venditti

Scanu

Santoro

et al. 2012

Science

162

188

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Newly synthesized proteins exit the endoplasmic reticulum (ER) via coat protein complex II (COPII) vesicles. Procollagen (PC), however, forms prefibrils that are too large to fit into typical COPII vesicles; PC thus needs large transport carriers, which we term megacarriers. TANGO1 assists PC packing, but its role in promoting the growth of megacarriers is not known. We found that TANGO1 recruited Sedlin, a TRAPP component that is defective in spondyloepiphyseal dysplasia tarda (SEDT), and that Sedlin was required for the ER export of PC. Sedlin bound and promoted efficient cycling of Sar1, a guanosine triphosphatase that can constrict membranes, and thus allowed nascent carriers to grow and incorporate PC prefibrils. This joint action of TANGO1 and Sedlin sustained the ER export of PC, and its derangement may explain the defective chondrogenesis underlying SEDT.

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“…More recently, Tca17 (TRAPPC2L in mammals), a protein with sequence similarity to Trs20, has been shown to be a substoichiometric component of TRAPPII and has been .proposed to play a role in promoting assembly and stability of TRAPPII13,14. TRAPPII binds to coatomer, the heptameric complex that forms the coat of COPI vesicles15,16, and it has been proposed to function in intra-Golgi and endosome-to-Golgi transport.…”

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confidence: 99%

Molecular architecture of the TRAPPII complex and implications for vesicle tethering

Yip

Berscheminski

Walz

2010

Nat Struct Mol Biol

105

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Multi-subunit tethering complexes participate in the process of vesicle tethering, the initial interaction between transport vesicles and their acceptor compartments. TRAPPII is a highly conserved tethering complex that functions in the late Golgi and consists of all TRAPPI and three specific subunits. We have purified native yeast TRAPPII and characterized its structure and subunit organization by single-particle electron microscopy. Our data show that the nine TRAPPII components form a core complex that dimerizes into a three-layered, diamond-shaped structure. The TRAPPI subunits assemble into TRAPPI complexes that form the outer layers. The three TRAPPII-specific subunits cap the ends of TRAPPI and form the middle layer responsible for dimerization. TRAPPII binds Ypt1 and likely uses the TRAPPI catalytic core to promote guanine nucleotide exchange. We discuss implications of the TRAPPII structure for coat interaction and TRAPPII-associated human pathologies.

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TRAPPC2L is a Novel, Highly Conserved TRAPP‐Interacting Protein

Cited by 49 publications

References 51 publications

Bi-allelic mutations in TRAPPC2L result in a neurodevelopmental disorder and have an impact on RAB11 in fibroblasts

Bi-allelic mutations in TRAPPC2L result in a neurodevelopmental disorder and have an impact on RAB11 in fibroblasts

Sedlin Controls the ER Export of Procollagen by Regulating the Sar1 Cycle

Molecular architecture of the TRAPPII complex and implications for vesicle tethering

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