Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins (Q28206094)

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Kerry Bruns

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Pradipta Ghosh

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Stuart Kornfeld

Journal of Biological Chemistry

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language of work or name

English

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publication date

24 May 2002

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published in

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volume

277

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issue

21

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page(s)

18477-82

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cites work

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Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors

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GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex

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A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome

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A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi

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Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin

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A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins

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Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi

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Sorting of mannose 6-phosphate receptors mediated by the GGAs

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Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor

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The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein

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Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains

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The GGAs promote ARF-dependent recruitment of clathrin to the TGN

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Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain

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Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites.

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A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes

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Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains

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Structural basis for recognition of acidic-cluster dileucine sequence by GGA1

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The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi

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Identification of three internalization sequences in the cytoplasmic tail of the 46 kDa mannose 6-phosphate receptor

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Serine phosphorylation site of the 46-kDa mannose 6-phosphate receptor is required for transport to the plasma membrane in Madin-Darby canine kidney and mouse fibroblast cells

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Mutations in the cytoplasmic domain of the 275 kd mannose 6-phosphate receptor differentially alter lysosomal enzyme sorting and endocytosis

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Systematic mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor cytoplasmic domain. An acidic cluster containing a key aspartate is important for function in lysosomal enzyme sorting

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The 46-kDa mannose 6-phosphate receptor contains multiple binding sites for clathrin adaptors

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Identifiers

DOI

10.1074/JBC.M201879200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11886874

1 reference

Consolidated OpenCitations Corpus – April 2017