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
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Research Support, Non-U.S. Gov't
MeSH terms
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Active Transport, Cell Nucleus / physiology
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Nucleus / metabolism*
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DNA-Binding Proteins / metabolism
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Galactosidases / genetics
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Galactosidases / metabolism
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Genetic Complementation Test / methods
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HeLa Cells
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Humans
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Mice
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Molecular Sequence Data
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NIH 3T3 Cells
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Neuropeptides / chemistry*
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Neuropeptides / genetics
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Neuropeptides / metabolism*
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Nuclear Localization Signals
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Trans-Activators / chemistry*
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Trans-Activators / genetics
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Trans-Activators / metabolism*
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Transfection
Substances
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DNA-Binding Proteins
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Neuropeptides
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Nuclear Localization Signals
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Nuclear Proteins
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Recombinant Fusion Proteins
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Trans-Activators
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Galactosidases