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Search: authors:"Matthew N. J. Seaman"

10 papers found.
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Analysis of novel endosome-to-Golgi retrieval genes reveals a role for PLD3 in regulating endosomal protein sorting and amyloid precursor protein processing

Matthew NJSeaman 0 -phosphate receptor GFP Green fluorescent protein 0 Sortilin-like 0 0 Cambridge Institute for Medical Research, Cambridge Biomedical Campus, University of Cambridge , Wellcome Trust

The retromer complex – endosomal protein recycling and beyond

Matthew N. J. Seaman 0 0 University of Cambridge, Cambridge Institute for Medical Research, and Department of Clinical Biochemistry, Addenbrooke's Hospital , Hills Road, Cambridge CB2 0XY, UK - to

RME-8 coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation

Caroline L. Freeman 0 Geoffrey Hesketh 0 Matthew N. J. Seaman 0 0 University of Cambridge, Cambridge Institute for Medical Research/Department of Clinical Biochemistry , Wellcome Trust/MRC Building

Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval

Matthew N. J. Seaman 0 0 University of Cambridge, Cambridge Institute for Medical Research/Clinical Biochemistry, Wellcome Trust/MRC building, Addenbrookes Hospital , Cambridge, CB2 0XY , UK

N-acetylation and phosphorylation of Sec complex subunits in the ER membrane

Background Covalent modifications of proteins provide a mechanism to control protein function. Here, we have investigated modifications of the heptameric Sec complex which is responsible for post-translational protein import into the endoplasmic reticulum (ER). It consists of the Sec61 complex (Sec61p, Sbh1p, Sss1p) which on its own mediates cotranslational protein import into...

The Fifth Adaptor Protein Complex

Adaptor protein (AP) complexes sort cargo into vesicles for transport from one membrane compartment of the cell to another. Four distinct AP complexes have been identified, which are present in most eukaryotes. We report the existence of a fifth AP complex, AP-5. Tagged AP-5 localises to a late endosomal compartment in HeLa cells. AP-5 does not associate with clathrin and is...

VPS29 Is Not an Active Metallo-Phosphatase but Is a Rigid Scaffold Required for Retromer Interaction with Accessory Proteins

VPS29 is a key component of the cargo-binding core complex of retromer, a protein assembly with diverse roles in transport of receptors within the endosomal system. VPS29 has a fold related to metal-binding phosphatases and mediates interactions between retromer and other regulatory proteins. In this study we examine the functional interactions of mammalian VPS29, using X-ray...