Description
Scribble, a member of the LAP protein family, contributes to the apicobasal polarity
(ABP) of epithelial cells. The LAP unique region (LUR) of these proteins is essential for
ABP function, and includes a highly conserved Leucine Reach Repeat (LRR) domain.
Here we study how the LRR domain of Scribble maintains ABP. We show that its
concave surface participates in three types of mutually exclusive interactions 1.
homodimerization serving as an auto-inhibitory mechanism, 2. interactions with a
diverse set of polarity proteins, such as Llgl1, Llgl2, EPB41L2 and EPB41L5, which
produce distinct multiprotein complexes, and 3. a direct interaction with the protein
phosphatase, PP1, which forms a dimeric LRR domain-PP1 complex. Our results suggest
that the latter complex maintains PP1 in the basolateral cell cortex in close proximity to
PP1 targets. Such organization generates a dynamic network where PP1 could be
immediately dispatched from the Scribble-PP1 complex to particular protein ligands.
This mechanism for controlling dephosphorylation kinetics of phosphorylated proteins
could be universal for all members of the LAP protein family, which includes Erbin,
Lano, and the neuron-specific protein, Densin-180.
[doi:10.25345/C5NZ6B]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Scribble, Apicobasal Polarity, Phosphatase PP1
Contact
Principal Investigators:
(in alphabetical order)
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Sergey M Troyanovsky, Northwestern University, United States
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Submitting User: |
indrajyoti
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"N/A" means no results of this type were submitted.
Originally identified proteins that were automatically
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SwissProt
human reference database.
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Number of distinct protein accessions reported across all analyses (original submission and
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Number of distinct unmodified peptide sequences reported across all analyses (original
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Number of distinct peptide sequences (including modified variants or peptidoforms) reported
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Total number of peptide-spectrum matches (i.e. spectrum identifications) reported across all
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Number of distinct proteins quantified across all analyses (original submission and reanalyses)
associated with this dataset.
Distinct protein accessions are counted across all files submitted in the "Statistical Analysis
of Quantified Analytes" category having a "Protein" column in this dataset.
"N/A" means no results of this type were submitted.
Number of distinct proteins found to be differentially abundant in at least one comparison
across all analyses (original submission and reanalyses) associated with this dataset.
A protein is differentially abundant if its change in abundance across conditions is found
to be statistically significant with an adjusted p-value <= 0.05 and lists no issues associated
with statistical tests for differential abundance.
Distinct protein accessions are counted across all files submitted in the "Statistical Analysis
of Quantified Analytes" category having a "Protein" column in this dataset.
"N/A" means no results of this type were submitted.
This dataset may not contain all raw spectra data as originally deposited in PRIDE.
It has been imported to MassIVE for reanalysis purposes, so its spectra data here may
consist solely of processed peak lists suitable for reanalysis with most software.