ArticleMolecular and cellular biology2002
A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
59 citing papers in PubMed, 143 citations in OpenAlex.
- Review
- Diverse Clinical Phenotypes ofGenes · 2023Review
- Article
- Mechanoregulation of PDZ Proteins, An Emerging Function.Methods in molecular biology (Clifton, N.J.) · 2021Review
- A role for alternative splicing in circadian control of exocytosis and glucose homeostasis.Genes & development · 2020Article
- LDL receptor related protein 1 requires the IBiochimica et biophysica acta. Molecular cell research · 2019Article
- Scaffold protein Lin7 family in membrane skeletal protein complex in mouse seminiferous tubules.Histochemistry and cell biology · 2019Article
- Scribble co-operatively binds multiple αScientific reports · 2019Article
- The interaction between CASK and the tumour suppressor Dlg1 regulates mitotic spindle orientation in mammalian epithelia.Journal of cell science · 2019Article
- SAP102 regulates synaptic AMPAR function through a CNIH-2-dependent mechanism.Journal of neurophysiology · 2018Article
- Novel CASK mutations in cases with syndromic microcephaly.Human mutation · 2018Article
- Palmitoylation regulates glutamate receptor distributions in postsynaptic densities through control of PSD95 conformation and orientation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Presynaptic DLG regulates synaptic function through the localization of voltage-activated Ca(2+) Channels.Scientific reports · 2016Article
- Immunohistochemical study of the membrane skeletal protein, membrane protein palmitoylated 6 (MPP6), in the mouse small intestine.Histochemistry and cell biology · 2016Article
- Structure-function analysis of SAP97, a modular scaffolding protein that drives dendrite growth.Molecular and cellular neurosciences · 2015Article
- Article
- Article
- Regulation of potassium channel trafficking in the distal nephron.Current opinion in nephrology and hypertension · 2013Review
- Cell polarity and cystic kidney disease.Pediatric nephrology (Berlin, Germany) · 2013Review
- CASK regulates SAP97 conformation and its interactions with AMPA and NMDA receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Mammalian Lin-2 (mLin-2)/CASK is a membrane-associated guanylate kinase (MAGUK) and contains multidomain modules that mediate protein-protein interactions important for the establishment and maintenance of neuronal and epithelial cell polarization. The importance of mLin-2/CASK in mammalian development is demonstrated by the fact that mutations in mLin-2/CASK or SAP97, another MAGUK protein, lead to cleft palate in mice. We recently identified a new protein-protein interaction domain, called the L27 domain, which is present twice in mLin-2/CASK. In this report, we further define the binding of the L27C domain of mLin-2/CASK to the L27 domain of mLin-7 and identify the binding partner for L27N of mLin-2/CASK. Biochemical analysis reveals that this L27N domain binds to the N terminus of SAP97, a region that was previously reported to be essential for the lateral membrane recruitment of SAP97 in epithelia. Our colocalization studies, using dominant-negative mLin-2/CASK, show that the association with mLin-2/CASK is crucial for lateral localization of SAP97 in MDCK cells. We also report the identification of a novel isoform of Discs Large, a Drosophila melanogaster orthologue of SAP97, which contains a region highly related to the SAP97 N terminus and which binds Camguk, a Drosophila orthologue of mLin-2/CASK. Our data identify evolutionarily conserved protein-protein interaction domains that link mLin-2/CASK to SAP97 and account for their common phenotype when mutated in mice.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.