Structural requirements for nuclear localization of GCMa/Gcm-1

FEBS Lett. 2003 Oct 23;553(3):315-20. doi: 10.1016/s0014-5793(03)01037-8.

Abstract

GCM proteins constitute a small transcription factor family. Nuclear localization of Drosophila GCM is mediated by a typical bipartite nuclear localization sequence (NLS) close to the DNA-binding GCM domain. Here, we have analyzed nuclear localization of the mammalian GCM proteins. Whereas GCMb/Gcm-2 contained a classical bipartite NLS, nuclear localization of GCMa/Gcm-1 was mediated by two regions without resemblance to known NLS, one corresponding to the amino-terminal part of the GCM domain, the second defined as a tyrosine-and-proline-rich carboxy-terminal region. Nuclear import was counteracted by an amino-terminal nuclear export activity. This complex regulation of subcellular localization has important implications for GCMa/Gcm-1 function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus / physiology
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Nucleus / metabolism*
  • DNA-Binding Proteins / metabolism
  • Galactosidases / genetics
  • Galactosidases / metabolism
  • Genetic Complementation Test / methods
  • HeLa Cells
  • Humans
  • Mice
  • Molecular Sequence Data
  • NIH 3T3 Cells
  • Neuropeptides / chemistry*
  • Neuropeptides / genetics
  • Neuropeptides / metabolism*
  • Nuclear Localization Signals
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Trans-Activators / chemistry*
  • Trans-Activators / genetics
  • Trans-Activators / metabolism*
  • Transfection

Substances

  • DNA-Binding Proteins
  • Neuropeptides
  • Nuclear Localization Signals
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Trans-Activators
  • Galactosidases