Adaptor-related proteins

Robinson, Margaret S.; Bonifacino, Juan S.

doi:10.1016/s0955-0674(00)00235-0

Cited by 495 publications

(446 citation statements)

References 88 publications

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“…46). Live cell spinning disc confocal imaging revealed that acute perturbation of clathrin TD function by Pitstop-2 interfered with the dynamics of GGA1-eGFP, GGA2-eGFP, and GGA3-eGFP positive structures (Fig.…”

Section: Reduced Mobility Of Ap-1-and Gga-coated Carriers Uponmentioning

confidence: 91%

Clathrin Terminal Domain-Ligand Interactions Regulate Sorting of Mannose 6-Phosphate Receptors Mediated by AP-1 and GGA Adaptors

Stahlschmidt

Robertson

Robinson

et al. 2014

Journal of Biological Chemistry

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Background: Clathrin is a coat protein involved in intracellular membrane traffic. Results: Acute inhibition of clathrin-ligand association by Pitstop compounds perturbs intracellular receptor sorting mediated by AP-1 and GGA adaptors. Conclusion: Clathrin is required for intracellular receptor sorting by AP-1 and GGA adaptor proteins. Significance: Pitstop compounds are tools for the functional dissection of intracellular trafficking pathways.

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Section: Reduced Mobility Of Ap-1-and Gga-coated Carriers Uponmentioning

confidence: 91%

Clathrin Terminal Domain-Ligand Interactions Regulate Sorting of Mannose 6-Phosphate Receptors Mediated by AP-1 and GGA Adaptors

Stahlschmidt

Robertson

Robinson

et al. 2014

Journal of Biological Chemistry

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“…Recently the structures of two other appendage domains have been solved: the AP-1 ␥ appendage and the GGA1 appendage (Kent et al, 2002;Lui et al, 2003;Nogi et al, 2002). The GGAs are monomeric adaptors that facilitate cargo selection at the TGN (Robinson and Bonifacino, 2001). AP-1 was also initially assumed to act at the TGN, although recent studies suggest that it may be more important in retrieving cargo from a post-TGN compartment (Meyer et al, 2000(Meyer et al, , 2001Valdivia et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

EpsinR: an ENTH Domain-containing Protein that Interacts with AP-1

Hirst

Motley

Harasaki

et al. 2003

MBoC

198

206

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We have used GST pulldowns from A431 cell cytosol to identify three new binding partners for the ␥-adaptin appendage: Snx9, ARF GAP1, and a novel ENTH domain-containing protein, epsinR. EpsinR is a highly conserved protein that colocalizes with AP-1 and is enriched in purified clathrin-coated vesicles. However, it does not require AP-1 to get onto membranes and remains membrane-associated in AP-1-deficient cells. Moreover, although epsinR binds AP-1 via its COOH-terminal domain, its NH 2 -terminal ENTH domain can be independently recruited onto membranes, both in vivo and in vitro. Brefeldin A causes epsinR to redistribute into the cytosol, and recruitment of the ENTH domain requires GTP␥S, indicating that membrane association is ARF dependent. In protein-lipid overlay assays, the epsinR ENTH domain binds to PtdIns(4)P, suggesting a possible mechanism for ARF-dependent recruitment onto TGN membranes. When epsinR is depleted from cells by RNAi, cathepsin D is still correctly processed intracellularly to the mature form. This indicates that although epsinR is likely to be an important component of the AP-1 network, it is not necessary for the sorting of lysosomal enzymes.

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“…The interaction of clathrin with membrane lipids and receptors destined for internalization is not direct but mediated by adaptor proteins (APs). In mammalian cells, there are four principal heterotetrameric adaptor protein complexes (AP1, AP2, AP3, and AP4), and each of them participates at distinct membrane traffic events at distinct sites of the cell (Robinson and Bonifacino, 2001). The adaptor complex AP2, which is composed of two large (␣-and ␤2-), a medium ( 2-), and a small ( 2)-subunit, recruits clathrin to the plasma membrane as a prerequisite for receptor-mediated endocytosis.…”

Section: Introductionmentioning

confidence: 99%