Proteomics

Dataset Information

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The tumor suppressor SCRIB is a negative modulator of the Wnt/-catenin signaling (part 1)


ABSTRACT: Epithelial tissues are highly organized structures that rely on cell polarity pathways driven by membrane receptors and scaffolding proteins. SCRIBBLE is a cytoplasmic scaffold present at cell-cell junctions in polarized cells that contains LRR and PDZ domains as its paralogue LANO, a member of the LAP protein family. The family is composed of DENSIN-180, ERBIN, SCRIB and LRRC1. Based on phylogenic tree, LAP proteins can be split in two branches with the first branch is made up with SCRIB and LRCC1 and the second one of ERBIN and DENSIN-180. The current interactome of SCRIB and LRRC1 consists of 67 and 30 protein interaction partners respectively with only 9 (10%) common partners (BioGRID, version 3.5). Our study uncovers the proteome associated to SCRIB and LRRC1 and described for the first time protein associated to each paralogue.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hek-293t Cell

SUBMITTER: Luc Camoin  

LAB HEAD: Luc Camoin

PROVIDER: PXD013647 | Pride | 2019-09-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Controle_Rep1.raw Raw
Controle_Rep1_20190221041711.raw Raw
Controle_Rep1_20190221065258.raw Raw
Controle_Rep2.raw Raw
Controle_Rep2_20190221152438.raw Raw
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Publications

The Tumor Suppressor SCRIB is a Negative Modulator of the Wnt/β-Catenin Signaling Pathway.

Daulat Avais M AM   Wagner Mônica Silveira MS   Walton Alexandra A   Baudelet Emilie E   Audebert Stéphane S   Camoin Luc L   Borg Jean-Paul JP  

Proteomics 20191020 21-22


SCRIB is a scaffold protein containing leucine-rich repeats (LRR) and PSD-95/Dlg-A/ZO-1 domains (PDZ) that localizes at the basolateral membranes of polarized epithelial cells. Deregulation of its expression or localization leads to epithelial defects and tumorigenesis in part as a consequence of its repressive role on several signaling pathways including AKT, ERK, and HIPPO. In the present work, a proteomic approach is used to characterize the protein complexes associated to SCRIB and its paral  ...[more]

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