Nopp 140 shuttles on tracks between nucleolus and cytoplasm

U. Thomas Meier, Günter Blobel

Research output: Contribution to journalArticle

315 Citations (Scopus)

Abstract

Nopp140 is a nucleolar phosphoprotein of 140 kd that we originally identified and purified as a nuclear localization signal (NLS)-binding protein. Molecular characterization revealed a 10-fold repeated motif of highly conserved acidic serine clusters that contain an abundance of phosphorylation consensus sites for casein kinase II (CK II). Indeed, Nopp140 is one of the most phosphoryaated proteins in the cell, and NLS binding was dependent on phosphorylation. Nopp140 was shown to shuttle between the nucleolus and the cytoplasm. Shuttling is likely to proceed on tracks that were revealed by immunoelectron microscopy. These tracks extend from the dense fibrillar component of the nucleolus across the nucleoplasm to some nuclear pore complexes. We suggest that Nopp140 functions as a chaperone for import into and/or export from the nucleolus.

Original languageEnglish (US)
Pages (from-to)127-138
Number of pages12
JournalCell
Volume70
Issue number1
DOIs
StatePublished - Jul 10 1992
Externally publishedYes

Fingerprint

Phosphorylation
Cytoplasm
alpha Karyopherins
Nuclear Pore
Casein Kinase II
Nuclear Localization Signals
Immunoelectron Microscopy
Phosphoproteins
Serine
Microscopic examination
Proteins

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Nopp 140 shuttles on tracks between nucleolus and cytoplasm. / Meier, U. Thomas; Blobel, Günter.

In: Cell, Vol. 70, No. 1, 10.07.1992, p. 127-138.

Research output: Contribution to journalArticle

Meier, U. Thomas ; Blobel, Günter. / Nopp 140 shuttles on tracks between nucleolus and cytoplasm. In: Cell. 1992 ; Vol. 70, No. 1. pp. 127-138.
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