The DOI matches its Crossref record; 29 of the 30 references it cites were found in a registry or an index.
Mammalian Scribble Forms a Tight Complex with the βPIX Exchange Factor
Open accessAbstract
Drosophila Scribble is implicated in the development of normal synapse structure and epithelial tissues, but it remains unclear how it plays a role and which process it controls. The mammalian homolog of Scribble, hScrib, has a primary structure and subcellular localization similar to that of its fly homolog, but its function remains unknown. Here we have used tandem mass spectrometry to identify major components of the hScrib network. We show that it includes betaPIX (also called Cool-1), a guanine nucleotide exchange factor (GEF), and its partner GIT1 (also called p95-APP1), a GTPase activating protein (GAP). betaPIX directly binds to the hScrib PDZ domains, and the hScrib/betaPIX complex is efficiently recovered in epithelial and neuronal cells and tissues. In cerebellar granule cell cultures, hScrib and betaPIX are both partially localized at neuronal presynaptic compartments. Furthermore, we show that hScrib is required to anchor betaPIX at the cell cortex and that dominant-negative betaPIX or hScrib proteins can each inhibit Ca2+-dependent exocytosis in neuroendocrine PC12 cells, demonstrating a functional relationship between these proteins. These data reveal the existence of a tight hScrib/betaPIX interaction and suggest that this complex potentially plays a role in neuronal transmission.
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“A specific point mutation within LRR13 (Prol 305 to Leu, P305L) of the human SCRIB protein (hSCRIB) has also been shown to abrogate membrane localization (13), disrupting recruitment of βPIX, and exocytosis.”
From Mislocalization of the Cell Polarity Protein Scribble Promotes Mammary Tumorigenesis and Is Associated with Basal Breast Cancer (2014) · cites this paper as [13]
In the citing paper
“Scribble is an integral component of synaptic protein complexes and can coimmunoprecipitate with β-catenin, the ADP-ribosylation factor-1 GTPase-activating protein (GAP) GIT1, the Rac/Cdc42 guanine nucleotide exchange factor β-PIX, and transmembrane receptor Neurexin (Audebert et al., 2004; Sun et al., 2009; Sun and Bamji, 2011; Rui et al., 2017).”
From Scribble: A master scaffold in polarity, adhesion, synaptogenesis, and proliferation (2019) · cites this paper as Audebert et al., 2004
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Metadata
- Authors
- Audebert, S., Navarro, C., Nourry, C., Chasserot-Golaz, S., Lécine, P., Bellaiche, Y., Dupont, J.-L., Premont, R. T., Sempéré, C., Strub, J.-M., Van Dorsselaer, A., Vitale, N., & Borg, J.-P.
- Affiliations
- Inserm (FR)
- Centre National de la Recherche Scientifique (FR)
- Duke Medical Center (US)
- Corresponding author
- Borg, Jean-Paul
- ORCID
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2004-06
- Volume
- 14
- Issue
- 11
- Pages
- 987-995
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2007101096
- Cited by
- 218
- References
- 30
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 2 · 2022: 4 · 2021: 10 · 2020: 9 · 2019: 10 · 2018: 11 · 2017: 10 · 2016: 12 · 2015: 9 · 2014: 15 · 2013: 11 · 2012: 14
- FWCI
- 5.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3333 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- Scribble, betaPIX, GIT1, PDZ domain, guanine nucleotide exchange factor, GTPase-activating protein, protein-protein interaction, presynaptic complex, exocytosis, neural transmission, cell cortex, cerebellar granule cells, synaptic structure, epithelium
- MeSH terms
- Cell Membrane, Cells, Cultured, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Exocytosis, Humans, Membrane Proteins, Phosphoproteins, Precipitin Tests, Mass Spectrometry, Presynaptic Terminals, DNA, Complementary, Cell Cycle Proteins, Reverse Transcriptase Polymerase Chain Reaction, Guanine Nucleotide Exchange Factors, GTPase-Activating Proteins, Two-Hybrid System Techniques, Tumor Suppressor Proteins, Adaptor Proteins, Signal Transducing, Rho Guanine Nucleotide Exchange Factors
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