ArticleThe Biochemical journal2004
Exchange protein directly activated by cAMP (EPAC) interacts with the light chain (LC) 2 of MAP1A.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- The Role of Epac in Cancer Progression.International journal of molecular sciences · 2020Review
- Genome-Wide Mapping Defines a Role for C/EBPβ and c-Jun in Non-Canonical Cyclic AMP Signalling.Cells · 2019Article
- Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development.Physiological reviews · 2018Review
- Review
- The cAMP sensors, EPAC1 and EPAC2, display distinct subcellular distributions despite sharing a common nuclear pore localisation signal.Cellular signalling · 2015Article
- Single-cell analyses of transcriptional heterogeneity during drug tolerance transition in cancer cells by RNA sequencing.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Regulation of the inflammatory response of vascular endothelial cells by EPAC1.British journal of pharmacology · 2012Review
- Article
- Emerging themes of cAMP regulation of the pulmonary endothelial barrier.American journal of physiology. Lung cellular and molecular physiology · 2011Review
- AKAP9 regulation of microtubule dynamics promotes Epac1-induced endothelial barrier properties.Blood · 2011Article
- Spatial regulation of cyclic AMP-Epac1 signaling in cell adhesion by ERM proteins.Molecular and cellular biology · 2010Article
- The interaction of Epac1 and Ran promotes Rap1 activation at the nuclear envelope.Molecular and cellular biology · 2010Article
- EPAC proteins transduce diverse cellular actions of cAMP.British journal of pharmacology · 2009Review
- MAP2-mediated in vitro interactions of brain microtubules and their modulation by cAMP.European biophysics journal : EBJ · 2009Article
- Prostaglandin E2 inhibits specific lung fibroblast functions via selective actions of PKA and Epac-1.American journal of respiratory cell and molecular biology · 2008Article
- Epac: effectors and biological functions.Naunyn-Schmiedeberg's archives of pharmacology · 2008Review
- Epac-selective cAMP analogs: new tools with which to evaluate the signal transduction properties of cAMP-regulated guanine nucleotide exchange factors.Cellular signalling · 2008Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using EPAC1 (exchange protein directly activated by cAMP 1) as bait in two-hybrid screens of foetal and adult human brain libraries, we identified the LC2 (light chain 2) of MAP1A (microtubule-associated protein 1A) as a protein capable of interaction with EPAC1. We applied an immunoprecipitation assay to demonstrate protein interaction between EPAC1 and LC2 in co-transfected human embryonic kidney 293 cells. EPAC2 also co-immunoprecipitated with LC2 from extracts of rat cerebellum. Immunolocalization in co-transfected human embryonic kidney 293 cells revealed that EPAC1 co-localizes with LC2 throughout the cell body. We found that endogenous EPAC2 is also immunolocalized with LC2 in PC12 cells. Immunolocalization of EPAC1 in transfected COS1 cells showed that EPAC1 is associated with the perinuclear region surrounding the nucleus and filamentous structures throughout the cell. Removal of the cAMP-binding domain of EPAC1 (DeltacAMP-EPAC1) appeared to disrupt targeting of EPAC1 in cells resulting in a more dispersed staining pattern. Using two-hybrid assay, we tested the ability of LC2 to interact with DeltacAMP-EPAC1 and DeltaDEP-EPAC1, which lacks a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain). We found that deletion of the cAMP-binding domain inhibited interaction between EPAC1 and LC2 in a two-hybrid assay, but removal of the DEP domain had little effect. LC2 was found to interact with a glutathione-S-transferase-fusion protein of the cAMP-binding domain of EPAC1 in a pull-down assay, but not the DEP, REM (Ras exchange motif) or CAT (catalytic) domains. Together with our two-hybrid results, this suggests that the cAMP-binding domain of EPAC1 mediates interaction with LC2.
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