ArticleNature communications2019
Mechanism of IRSp53 inhibition by 14-3-3.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 60 citations in OpenAlex.
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- A NanoCurvS platform for quantitative and multiplex analysis of curvature-sensing proteins.Biomaterials science · 2023Article
- Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling.Nature communications · 2023Article
- Autonomous Synthesis of Functional, Permanently Phosphorylated Proteins for Defining the Interactome of Monomeric 14-3-3ζ.ACS central science · 2023Article
- Accessing isotopically labeled proteins containing genetically encoded phosphoserine for NMR with optimized expression conditions.The Journal of biological chemistry · 2022Article
- Expression of actin- and oxidative phosphorylation-related transcripts across the cortical visuospatial working memory network in unaffected comparison and schizophrenia subjects.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2022Article
- Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions.Science advances · 2022Article
- Contemporary biophysical approaches for studying 14-3-3 protein-protein interactions.Frontiers in molecular biosciences · 2022Review
- Identification of HCN1 as a 14-3-3 client.PloS one · 2022Article
- PermaPhosbioRxiv : the preprint server for biology · 2021Article
- Novel human cell expression method reveals the role and prevalence of posttranslational modification in nonmuscle tropomyosins.The Journal of biological chemistry · 2021Article
- Pathways to Parkinson's disease: a spotlight on 14-3-3 proteins.NPJ Parkinson's disease · 2021Review
- Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions.Biochemical Society transactions · 2021Review
- Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53.eLife · 2021Article
- SH3BP4 promotes neuropilin-1 and α5-integrin endocytosis and is inhibited by Akt.Developmental cell · 2021Article
- BAIAP2L2 facilitates the malignancy of prostate cancer (PCa) via VEGF and apoptosis signaling pathways.Genes & genomics · 2021Article
- Different phosphorylation and farnesylation patterns tune Rnd3-14-3-3 interaction in distinct mechanisms.Chemical science · 2021Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Filopodia are precursors of dendritic spines and polarized cell migration. The I-BAR-domain protein IRSp53 is a key regulator of filopodia dynamics that couples Rho-GTPase signaling to cytoskeleton and membrane remodeling, playing essential roles in neuronal development and cell motility. Here, we describe the structural-functional basis for 14-3-3-dependent inhibition of IRSp53. Phosphoproteomics, quantitative binding and crystallographic studies demonstrate that 14-3-3 binds to two pairs of phosphorylation sites in IRSp53. Using bicistronic expression, we obtain an IRSp53 heterodimer in which only one subunit is phosphorylated, and show that each subunit of IRSp53 independently binds one 14-3-3 dimer. A FRET-sensor assay using natively phosphorylated IRSp53 reveals opposite conformational changes upon binding of activatory (Cdc42, Eps8) or inhibitory (14-3-3) inputs. Finally, we show that 14-3-3 inhibits IRSp53 binding to membranes. Collectively, our findings support a mechanism whereby phosphorylation-dependent inhibition of IRSp53 by 14-3-3 counters membrane binding and interactions with Cdc42 and downstream cytoskeletal effectors.
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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.