Tyrosine kinase regulation of nuclear envelope assembly

Richard D. Byrne, Banafshé Larijani, Dominic L. Poccia

Research output: Contribution to journalArticlepeer-review

8 Citations (SciVal)

Abstract

We have described the co-localization of PLCγ and SFK1/7 in vivo and in vitro, and demonstrated their recruitment together to nuclei during membrane binding. We hypothesize that SFK1/7 is activated in response to GTP hydrolysis, phosphorylating and priming PLCγ for activation and thus producing the fusogen DAG during NE assembly. In addition to enhancing our understanding of the temporal and spatial mechanisms of NE formation, this pathway offers a novel link between protein regulation and lipid metabolism that has implications for general membrane fusion events.

Original languageEnglish
Pages (from-to)148-156
Number of pages9
JournalAdvances in Enzyme Regulation
Volume49
Issue number1
DOIs
Publication statusPublished - 20 Jan 2009

Bibliographical note

Funding Information:
We are very grateful to Paul Davies of Macrae & Company for sea urchin procurement, Kathy Foltz for the kind gift of the AmPLCγpep and SFK1/7 antisera, Mike Mitchell (CR-UK, Bioinformatics & Biostatistics) for sea urchin genome analysis and Jackie Eastman for assistance with confocal microscopy. This work was supported by CR-UK and an Amherst College Faculty Research Award from the H. Axel Schupf '57 Fund for Intellectual Life (DLP). RDB was funded by an Amherst College Copeland Fellowship and CR-UK.

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Genetics
  • Cancer Research

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