Mouse Disabled1 (DAB1) Is a Nucleocytoplasmic Shuttling Protein

The POU protein Oct-6 is a nucleocytoplasmic shuttling protein

Like many POU domain proteins, Oct-6 plays important roles during vertebrate development. In accord with its function as a transcriptional regulator during neurogenesis and myelination, Oct-6 is predominantly found in the nucleus. Nuclear import is mediated by a nuclear localization signal at the N-terminal end of the POU homeodomain. Here we show, that Oct-6 in addition contains a nuclear expo...

Nucleocytoplasmic Shuttling of HMGB1 Is

hDbr1 is a nucleocytoplasmic shuttling protein with a protein phosphatase-like motif essential for debranching activity

In higher eukaryotes most genes contain multiple introns. Introns are excised from pre-mRNAs by splicing and eventually degraded in the nucleus. It is likely that rapid intron turnover in the nucleus is important in higher eukaryotes, but this pathway is poorly understood. In order to gain insights into this pathway, we analyzed the human lariat RNA debranching enzyme1 (hDbr1) protein that cata...

Nucleocytoplasmic Shuttling of Endocytic Proteins

Many cellular processes rely on the ordered assembly of macromolecular structures. Here, we uncover an unexpected link between two such processes, endocytosis and transcription. Many endocytic proteins, including eps15, epsin1, the clathrin assembly lymphoid myeloid leukemia (CALM), and alpha-adaptin, accumulate in the nucleus when nuclear export is inhibited. Endocytosis and nucleocytoplasmic ...

hMSH5 is a nucleocytoplasmic shuttling protein whose stability depends on its subcellular localization

MSH5 is a MutS-homologous protein required for meiotic DNA recombination. In addition, recent studies suggest that the human MSH5 protein (hMSH5) participates to mitotic recombination and to the cellular response to DNA damage and thus raise the possibility that a tight control of hMSH5 function(s) may be important for genomic stability. With the aim to characterize mechanisms potentially invol...