ArticleMolecular biology of the cell2001
Interaction with mLin-7 alters the targeting of endocytosed transmembrane proteins in mammalian epithelial cells.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 43 citations in OpenAlex.
- LIN-10 can promote LET-23 EGFR signaling and trafficking independently of LIN-2 and LIN-7.Molecular biology of the cell · 2021Article
- Golgi localization of the LIN-2/7/10 complex points to a role in basolateral secretion of LET-23 EGFR in theDevelopment (Cambridge, England) · 2021Article
- CASK (LIN2) interacts with Cx43 in wounded skin and their coexpression affects cell migration.Journal of cell science · 2012Article
- The avian influenza virus NS1 ESEV PDZ binding motif associates with Dlg1 and Scribble to disrupt cellular tight junctions.Journal of virology · 2011Article
- Sorting it out in endosomes: an emerging concept in renal epithelial cell transport regulation.Physiology (Bethesda, Md.) · 2010Review
- CASK deletion in intestinal epithelia causes mislocalization of LIN7C and the DLG1/Scrib polarity complex without affecting cell polarity.Molecular biology of the cell · 2009Article
- Biology and regulation of ectoplasmic specialization, an atypical adherens junction type, in the testis.Biochimica et biophysica acta · 2008Review
- Renal defects associated with improper polarization of the CRB and DLG polarity complexes in MALS-3 knockout mice.The Journal of cell biology · 2007Article
- TIP-1 has PDZ scaffold antagonist activity.Molecular biology of the cell · 2006Article
- Osmotic regulation of renal betaine transport: transcription and beyond.Pflugers Archiv : European journal of physiology · 2004Review
- The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost.The Journal of cell biology · 2002Article
- A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia.Molecular and cellular biology · 2002Article
- Regulation of actin dynamics and protein trafficking during spermatogenesis--insights into a complex process.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To investigate the targeting mechanism for proteins bound to the mammalian Lin-7 (mLin-7) PDZ domain, we created receptor protein chimeras composed of the carboxyl-terminal amino acids of LET-23 fused to truncated nerve growth factor receptor/P75. mLin-7 bound to the chimera with a wild-type LET-23 carboxyl-terminal tail (P75t-Let23WT), but not a mutant tail (P75t-Let23MUT). In Madin-Darby canine kidney (MDCK) cells, P75t-Let23WT localized to the basolateral plasma membrane domain, whereas P75t-Let23MUT remained apical. Furthermore, mutant mLin-7 constructs acted as dominant interfering proteins and inhibited the basolateral localization of P75t-Let23WT. The mechanisms for this differential localization were examined further, and, initially, we found that P75t-Let23WT and P75t-Let23MUT were delivered equally to the apical and basolateral plasma membrane domains. Although basolateral retention of P75t-Let23WT, but not P75t-Let23MUT, was observed, the greatest difference in receptor localization was seen in the rapid trafficking of P75t-Let23WT to the basolateral plasma membrane domain after endocytosis, whereas P75t-Let23MUT was degraded in lysosomes, indicating that mLin-7 binding can alter the fate of endocytosed proteins. Altogether, these data support a model for basolateral protein targeting in mammalian epithelial cells dependent on protein-protein interactions with mLin-7, and also suggest a dynamic role for mLin-7 in endosomal sorting.
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.