Review article

New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones

  1. Lindsay J. Frehlick1,
  2. José María Eirín-López1,2,
  3. Juan Ausió1,*

Article first published online: 22 DEC 2006

DOI: 10.1002/bies.20512

Issue

BioEssays

BioEssays

Volume 29, Issue 1, pages 49–59, January 2007

Additional Information

How to Cite

Frehlick, L. J., Eirín-López, J. M. and Ausió, J. (2007), New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones. Bioessays, 29: 49–59. doi: 10.1002/bies.20512

Author Information

  1. 1

    Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada

  2. 2

    Departamento de Biología Celular y Molecular, Universidade da Coruña, Spain

*Department of Biochemistry and Microbiology, University of Victoria, Petch Building, 258, Victoria, B.C., Canada V8W 3P6.

Publication History

  1. Issue published online: 22 DEC 2006
  2. Article first published online: 22 DEC 2006

Funded by

  • This work was supported by a grant from the Natural Sciences and Engineering Research Council of Canada (NSERC), Grant number OGP 0046399 (to J.A.), by a Postdoctoral Marie Curie International Fellowship within the 6th European Community Framework Programme (to J.M.E.-L) and by an NSERC postgraduate scholarship (to L.J.F.)

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Abstract

Basic proteins and nucleic acids are assembled into complexes in a reaction that must be facilitated by nuclear chaperones in order to prevent protein aggregation and formation of non-specific nucleoprotein complexes. The nucleophosmin/nucleoplasmin (NPM) family of chaperones [NPM1 (nucleophosmin), NPM2 (nucleoplasmin) and NPM3] have diverse functions in the cell and are ubiquitously represented throughout the animal kingdom. The importance of this family in cellular processes such as chromatin remodeling, genome stability, ribosome biogenesis, DNA duplication and transcriptional regulation has led to the rapid growth of information available on their structure and function. The present review covers different aspects related to the structure, evolution and function of the NPM family. Emphasis is placed on the long-term evolutionary mechanisms leading to the functional diversification of the family members, their role as chaperones (particularly as it pertains to their ability to aid in the reprogramming of chromatin), and the importance of NPM2 as an essential component of the amphibian chromatin remodeling machinery during fertilization and early embryonic development. BioEssays 29: 49–59, 2007. © 2006 Wiley Periodicals, Inc.

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