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Cytoplasmic interaction of the tumour suppressor protein hSNF5 with dynamin-2 controls endocytosis

T Alfonso-Pérez1, M S Domínguez-Sánchez1, M García-Domínguez2

  • 1Molecular Biology Department, Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER), Consejo Superior de Investigaciones Científicas (CSIC), Seville, Spain.

Oncogene
|July 16, 2013
PubMed

Insights

Human SNF5 protein shuttles to the cytoplasm, where it interacts with dynamin-2 (DNM2). This interaction stabilizes DNM2 and affects endocytosis, revealing a new role for SNF5 in tumor development.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Human SNF5 (hSNF5) is a key component of the SWI/SNF chromatin remodeling complex and a tumor suppressor.
  • Mutations in hSNF5 are linked to rhabdoid tumors and it also interacts with HIV-1 integrase.
  • hSNF5 shuttles between the nucleus and cytoplasm, prompting investigation into its cytoplasmic functions.

Purpose of the Study:

  • To investigate the cytoplasmic role of hSNF5.
  • To determine if hSNF5 interacts with other cytoplasmic proteins.
  • To elucidate the functional consequences of hSNF5's cytoplasmic localization on cellular processes.

Main Methods:

  • Fluorescence loss in photobleaching to track hSNF5 localization.
  • Co-immunoprecipitation to assess protein interactions.
  • Endocytosis assays and GTPase activity measurements.
  • siRNA-mediated depletion of hSNF5 and SWI/SNF components.

Main Results:

  • hSNF5 directly interacts with dynamin-2 (DNM2) in the cytoplasm and colocalizes with DNM2 in endocytic vesicles.
  • Depletion of hSNF5 destabilizes DNM2 and impairs DNM2-dependent endocytosis.
  • hSNF5 inhibits the assembly-stimulated GTPase activity of DNM2 in vitro.

Conclusions:

  • hSNF5 plays an unexpected role in regulating DNM2 stability and activity, thereby modulating endocytosis.
  • These findings provide new insights into the function of hSNF5 beyond chromatin remodeling and its potential role in tumor genesis.

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