Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1

Czubayko, Martin; Knauth, Peter; Schlüter, Thomas; Florian, Volker; Bohnensack, Ralf

doi:10.1016/j.bbrc.2006.04.129

Cited by 38 publications

(36 citation statements)

References 46 publications

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“…1), we hypothesized that SNX17 uses its FERM domain to bind KRIT1. This notion is supported by the previous report that the C-terminal portion of SNX17 containing the FERM-like domain (SNX17-FERM) mediates the interaction with KRIT1 (22). To investigate the molecular details of the interaction between SNX17 and KRIT1, we determined the co-crystal structure of the SNX17 FERM domain in complex with KRIT1 NPXF2 peptide.…”

Section: Snx17 Directly Binds Krit1 Npxf2 Motif-snx17 Has Beensupporting

confidence: 55%

“…Since the first report of an interaction between SNX17 and KRIT1 (22), no further studies have been presented. To gain a more complete understanding of how SNX17 interacts with KRIT1, we characterize the complex using biochemical, crystallographic, and biophysical approaches.…”

mentioning

confidence: 99%

“…Another reported cytoplasmic binding partner for SNX17 is Krev interaction trapped 1 (KRIT1) (22). The gene encoding KRIT1 is associated with cerebral cavernous malformations (CCM), a class of vascular dysplasias that cause mulberry-shaped lesions leading to increased risk of stroke (23); accordingly, KRIT1 is also commonly referred to as CCM1 (24).…”

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confidence: 99%

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Structural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)

Stiegler

Zhang

Liu

et al. 2014

Journal of Biological Chemistry

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Background: Sorting nexin 17 (SNX17) binds cytoplasmic proteins in addition to cell surface receptors. Results: A direct interaction between SNX17 and the cytoplasmic adaptor protein KRIT1 (Krev interaction trapped 1) is characterized by biochemistry and crystallography. Conclusion: KRIT1 is a SNX17 binding partner. Significance: Understanding the binding activities of SNX17 may suggest function beyond endosomal sorting.

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Section: Snx17 Directly Binds Krit1 Npxf2 Motif-snx17 Has Beensupporting

confidence: 55%

mentioning

confidence: 99%

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Structural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)

Stiegler

Zhang

Liu

et al. 2014

Journal of Biological Chemistry

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“…An IL-6-gp130-STAT3-mediated increase in cathepsin S activity reduces the MHCII alpha/beta dimer in Dendritic cells and suppresses CD4 + T cell-mediated immune responses [23] . SNX17, a non-selfassembling protein, interacts with KRIT1, which plays a role in cell adhesion processes and intergrin signaling [24] . It also has been identified as a novel interaction partner for members of the LDLR family.…”

Section: Discussionmentioning

confidence: 99%

Yeast two-hybrid screening of proteins interacting with plasmin receptor subunit: C-terminal fragment of annexin A2

Laumonnier

Syrovets

et al. 2011

Acta Pharmacol Sin

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Aim: To identify proteins that interact with the C-terminal fragment of annexin A2 (A2IC), generated by plasmin cleavage of the plasmin receptor, a heterotetramer (AA2t) containing annexin A2. Methods: The gene that encodes the A2IC fragment was obtained from PCR-amplified cDNA isolated from human monocytes, and was ligated into the pBTM116 vector using a DNA ligation kit. The resultant plasmid (pBTM116-A2IC) was sequenced with an ABI PRISM 310 Genetic Analyzer. The expression of an A2IC bait protein fused with a LexA-DNA binding domain (BD) was determined using Western blot analysis. The identification of proteins that interact with A2IC and are encoded in a human monocyte cDNA library was performed using yeast two-hybrid screening. The DNA sequences of the relevant cDNAs were determined using an ABI PRISM BigDye terminator cycle sequencing ready reaction kit. Nucleotide sequence databases were searched for homologous sequences using BLAST search analysis (http://www.ncbi.nlm.nih.gov). Confirmation of the interaction between the protein LexA-A2IC and each of cathepsin S and SNX17 was conducted using a small-scale yeast transformation and X-gal assay. Results: The yeast transformed with plasmids encoding the bait proteins were screened with a human monocyte cDNA library by reconstituting full-length transcription factors containing the GAL4-active domain (GAL4-AD) as the prey in a yeast two-hybrid approach. After screening 1×10 7 clones, 23 independent β-Gal-positive clones were identified. Sequence analysis and a database search revealed that 15 of these positive clones matched eight different proteins (SNX17, ProCathepsin S, RPS2, ZBTB4, OGDH, CCDC32, PAPD4, and actin which was already known to interact with annexin A2). Conclusion: A2IC A2IC interacts with various proteins to form protein complexes, which may contribute to the molecular mechanism of monocyte activation induced by plasmin. The yeast two-hybrid system is an efficient approach for investigating protein interactions.Keywords: yeast yeast two-hybrid system; human monocyte; plasmin receptor; C-terminal fragment of annexin A2 (A2IC); protein-protein interaction Acta

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“…Recycling of cargo proteins that contain NPxY-sorting motifs including β1-integrin (Bottcher, Stremmel et al 2012;Steinberg, Heesom et al 2012), LDLR (Burden, Sun et al 2004) and LRP1 (Donoso, Cancino et al 2009) in polarized and neuronal cells is mediated by SNX17 (Czubayko, Knauth et al 2006). Efficient SNX17-mediated β1-integrin recycling via Rab11-positive recycling endosomes en route to the cell surface prevents ubiquitylation of α-and β-integrin cytodomains and rapid lysosomal degradation.…”

Section: Figure 3: Tubular Cargo-enriched Subdomains At the Early Sormentioning

confidence: 99%

A phosphoinositide conversion mechanism for exit from endosomes

Ketel¹,

Krauß²,

Nicot³

et al. 2016

Nature

161

177

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I owe special thanks to Marnix Wieffer and Michael Krauß, who spent a lot of time helping me to get started in the lab, to overcome numerous experimental problem, I was not sure how to deal with, and frequently joined in discussions about my project with excellent advice. I am really grateful for your experimental support, Michael, and the time you invested in the project during our paper revision.Further, I would like to thank Jocelyn Laporte and his group, especially Anne-Sophie Nicot, at the IGBMC in Strasbourg for their support and a very fruitful collaboration, and Carsten Schultz and his group at the EMBL in Heidelberg for their support and constant supply with PIP/AMs. I owe special thanks to Dmytro Puchkov for the ultrastructural analysis and Eberhard Krause for mass spectrometry done within this project. I also need to acknowledge Markus Wenk and Federico Torta at the Singapore Lipidomics Incubator for joining the project at a very late stage, when we urgently needed help from lipidomics specialists. It was a pity that experiments did not work out as planned.I would further like to express my gratitude to two very skilled technicians in the AG Haucke lab: Silke Zillmann and Delia Löwe. Without your help it would have been impossible to achieve so much within the limited amount of time I had during the paper revision. by VPS34-IN1 treatment................................................... 52 2.3.11 Fluorescence microscopy................................................................................. 53 2.3.12 Flow cytometry............................................................................................ III SummaryPhosphoinositides (PIs) are a minor class of short-lived phospholipids that serve as crucial signposts of membrane identity. Thereby, PIs full fill important functions in cell signaling and membrane transport. PI 4-phosphates such as phosphatitylinositol-4-phosphate (PI(4)P) and phosphatitylinositol-4,5-bisphosphate (PI(4,5)P 2 ) are enriched at the plasma membrane (PM), on secretory organelles and lysosomes, while PI 3-phosphates, i.e.phosphatitylinositol-3-phosphate (PI(3)P), are a hallmark of the endosomal system.Directional transport between these compartments, thus, requires regulated PI conversion.However, PI conversion in exit from PI(3)P-enriched endosomes en route to the PI(4)P-and PI(4,5)P 2 -positive PM in endosomal recycling remained unknown.Here, we report that cargo exit from endosomes requires removal of PI(3)P by the PI(3)P 3-phosphatase myotubularin 1 (MTM1), and concomitant PI(4)P synthesis by PI 4-kinase type II α (PI4K2α). Loss of MTM1 causes endosomal accumulation of PI(3)P and PI(3)P effector proteins, i.e. sorting nexins, Kif16b-mediated outward traffic of PI(3)P containing endosomes and sub-plasmalemmal accumulation of exocytosis-deficient endosomes. As PI4K2α associates with MTM1 and thereby facilitates membrane recruitment of MTM1, these phenotypic changes are mimicked by loss of PI4K2α. The conversion of PI(3)P-to-PI(4)P is paralleled by a switch i...

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Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1

Cited by 38 publications

References 46 publications

Structural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)

Structural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)

Yeast two-hybrid screening of proteins interacting with plasmin receptor subunit: C-terminal fragment of annexin A2

A phosphoinositide conversion mechanism for exit from endosomes

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