ArticleMolecular and cellular biology1999
Identification of a new Pyk2 target protein with Arf-GAP activity.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 172 citations in OpenAlex.
- Dual targeting of interlocked PTK2B and MAPK signaling triggers synergistic ferroptosis via autophagic flux disruption in BRAFCell communication and signaling : CCS · 2026Article
- ASAP1 and ARF1 Regulate Myogenic Differentiation in Rhabdomyosarcoma by Modulating TAZ Activity.Molecular cancer research : MCR · 2025Article
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- PYK2 senses calcium through a disordered dimerization and calmodulin-binding element.Communications biology · 2022Article
- Nephrotoxicity evaluation and proteomic analysis in kidneys of rats exposed to thioacetamide.Scientific reports · 2022Article
- The novel driver gene ASAP2 is a potential druggable target in pancreatic cancer.Cancer science · 2021Article
- Crucial Players for Inter-Organelle Communication: PI5P4Ks and Their Lipid Product PI-4,5-PFrontiers in cell and developmental biology · 2021Article
- The Non-receptor Tyrosine Kinase Pyk2 in Brain Function and Neurological and Psychiatric Diseases.Frontiers in synaptic neuroscience · 2021Review
- Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019Review
- Selenoprotein K regulation of palmitoylation and calpain cleavage of ASAP2 is required for efficient FcγR-mediated phagocytosis.Journal of leukocyte biology · 2017Article
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- A Dual Role for the Nonreceptor Tyrosine Kinase Pyk2 during the Intracellular Trafficking of Human Papillomavirus 16.Journal of virology · 2015Article
- Proteomics in radiation research: present status and future perspectives.Radiation and environmental biophysics · 2014Review
- Striatal-enriched protein-tyrosine phosphatase (STEP) regulates Pyk2 kinase activity.The Journal of biological chemistry · 2012Article
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- Role for the SRC family kinase Fyn in sphingolipid acquisition by chlamydiae.Infection and immunity · 2011Article
- Recruitment of Pyk2 to SHPS-1 signaling complex is required for IGF-I-dependent mitogenic signaling in vascular smooth muscle cells.Cellular and molecular life sciences : CMLS · 2010Article
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- Targeting Pyk2 for therapeutic intervention.Expert opinion on therapeutic targets · 2010Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein tyrosine kinase Pyk2 is activated by a variety of G-protein-coupled receptors and by extracellular signals that elevate intracellular Ca2+ concentration. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. Immunofluorescence experiments demonstrate that Pap is localized in the Golgi apparatus and at the plasma membrane, where it is colocalized with Pyk2. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Addition of recombinant Pap protein to Golgi preparations prevented Arf-dependent generation of post-Golgi vesicles in vitro. Moreover, overexpression of Pap in cultured cells reduced the constitutive secretion of a marker protein. We propose that Pap functions as a GAP for Arf and that Pyk2 may be involved in regulation of vesicular transport through its interaction with Pap.
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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.