Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequence.

Humphrey, Jeffrey S.; Peters, Peter J.; Yuan, Lydia C.; Bonifacino, Juan S.

doi:10.1083/jcb.120.5.1123

Cited by 254 publications

(270 citation statements)

References 78 publications

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“…Signals such as the C-terminal tetrapeptide KDEL (Munro & Pelham, 1987) retrieve soluble proteins from the Golgi complex back to the ER lumen. Also the tetrapeptide YQRL is sufficient for trans-Golgi localization of proteins (Humphrey et al, 1993). Testing the levansucrase sequence for the presence of known retention signals did not reveal the presence of known ER or Golgi retention signals.…”

Section: Discussionmentioning

confidence: 97%

The vacuolar sorting domain of sporamin transports GUS, but not levansucrase, to the plant vacuole

TURK¹,

ROOS²,

SCOTTI³

et al. 1997

New Phytologist

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SUMMARYFructans (polyfructosylsucrose) are synthesized by a number of plants and micro-organisms. Plant fructans are localized in the vacuole and have a low degree of polymerization (DP), whereas the fructans synthesized by microorganisms are usually much bigger. There is an increasing interest in fructans for both food and non-food applications. In order to accumulate fructans of high DP in the plant vacuole, the levansucrase protein of Bacillus subtilis was fused to the vacuoiar targeting sequence of sporamin and expressed in plants. Transgenic tobacco plants in which this fusion gene is expressed accumulate fructans to levels up to 21 % of the d. w^t. They showed a reduced translocation of carbohydrates, bleaching of the leaves, stunted growth and increased levels of hexoses and starch. The levansucrase protein was not translocated to the plant vacuole, but retained in the endomembrane system, even though the same targeting signal was able to translocate the E. coli GUS protein to the plant vacuole.

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Section: Discussionmentioning

confidence: 97%

The vacuolar sorting domain of sporamin transports GUS, but not levansucrase, to the plant vacuole

TURK¹,

ROOS²,

SCOTTI³

et al. 1997

New Phytologist

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“…The YMPL motif resembles other Tyr-based motifs implicated in targeting to endosomes or the TGN and interaction with the clathrin-associated adaptor proteins (Bos et al, 1993;Humphrey et al, 1993;Wong and Hong, 1993;Ohno et al, 1995). Both of the Tyr-containing regions are conserved between AtELP and the maize EST clone.…”

Section: Dlscusslonmentioning

confidence: 99%

Cloning and Subcellular Location of an Arabidopsis Receptor-Like Protein That Shares Common Features with Protein-Sorting Receptors of Eukaryotic Cells

1997

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Many receptors involved in clathrin-mediated protein transport through the endocytic and secretory pathways of yeast and animal cells share common features. They are all type I integral membrane proteins containing cysteine-rich lumenal domains and cytoplasmic tails with tyrosine-containing sorting signals. The cysteine-rich domains are thought to be involved in ligand binding, whereas the cytoplasmic tyrosine motifs interact with clathrin-associated adaptor proteins during protein sorting along these pathways. In addition, tyrosine-containing signals are required for the retention and recycling of some of these membrane proteins to the trans-Golgi network. Here we report the characterization of an approximately 80-kD epidermal growth factor receptor-like type I integral membrane protein containing all of these functional motifs from Arabidopsis thaliana (called AtELP for A. thaliana Epidermal growth factor receptor-Like Protein). Biochemical analysis indicates that AtELP is a membrane protein found at high levels in the roots of both monocots and dicots. Subcellular fractionation studies indicate that the AtELP protein is present in two membrane fractions corresponding to a novel, undefined compartment and a fraction enriched in vesicles containing clathrin and its associated adaptor proteins. AtELP may therefore serve as a marker for compartments involved in intracellular protein trafficking in the plant cell.

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“…As an additional assay to better determine whether TOCA/CDC-42/PAR/WAVE proteins are required for transport of cargo from recycling endosomes to the TGN, we focused a set of experiments on TGN-38, the C. elegans homolog of mammalian TGN38/TGN46 (40)(41)(42). We focused on TGN-38 because previous work in mammalian cells showed that when its recycling is blocked, TGN38 accumulates in the compartment from which its budding is impaired, and because TGN38 is transported from the plasma membrane to the TGN via recycling endosomes (endocytic recycling compartment) in the well-studied CHO cell model (20, 22-24, 43, 44).…”

Section: Loss Ofmentioning

confidence: 99%

A TOCA/CDC-42/PAR/WAVE functional module required for retrograde endocytic recycling

Bai

Grant

2015

Proc. Natl. Acad. Sci. U.S.A.

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Endosome-to-Golgi transport is required for the function of many key membrane proteins and lipids, including signaling receptors, small-molecule transporters, and adhesion proteins. The retromer complex is well-known for its role in cargo sorting and vesicle budding from early endosomes, in most cases leading to cargo fusion with the trans-Golgi network (TGN). Transport from recycling endosomes to the TGN has also been reported, but much less is understood about the molecules that mediate this transport step. Here we provide evidence that the F-BAR domain proteins TOCA-1 and TOCA-2 (Transducer of Cdc42 dependent actin assembly), the small GTPase CDC-42 (Cell division control protein 42), associated polarity proteins PAR-6 (Partitioning defective 6) and PKC-3/atypical protein kinase C, and the WAVE actin nucleation complex mediate the transport of MIG-14/Wls and TGN-38/TGN38 cargo proteins from the recycling endosome to the TGN in Caenorhabditis elegans. Our results indicate that CDC-42, the TOCA proteins, and the WAVE component WVE-1 are enriched on RME-1-positive recycling endosomes in the intestine, unlike retromer components that act on early endosomes. Furthermore, we find that retrograde cargo TGN-38 is trapped in early endosomes after depletion of SNX-3 (a retromer component) but is mainly trapped in recycling endosomes after depletion of CDC-42, indicating that the CDC-42-associated complex functions after retromer in a distinct organelle. Thus, we identify a group of interacting proteins that mediate retrograde recycling, and link these proteins to a poorly understood trafficking step, recycling endosome-to-Golgi transport. We also provide evidence for the physiological importance of this pathway in WNT signaling.retromer | endocytic recycling | endosome | toca | wave

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Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequence.

Cited by 254 publications

References 78 publications

The vacuolar sorting domain of sporamin transports GUS, but not levansucrase, to the plant vacuole

The vacuolar sorting domain of sporamin transports GUS, but not levansucrase, to the plant vacuole

Cloning and Subcellular Location of an Arabidopsis Receptor-Like Protein That Shares Common Features with Protein-Sorting Receptors of Eukaryotic Cells

A TOCA/CDC-42/PAR/WAVE functional module required for retrograde endocytic recycling

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