Molecular dissection of nucleolin's role in growth and cell proliferation: new insights - PubMed

Affiliations

• PMID: 10544174

Review

Molecular dissection of nucleolin's role in growth and cell proliferation: new insights

M Srivastava et al. FASEB J. 1999 Nov.

Abstract

Cells require optimum protein synthetic activity in order to support cell proliferation, maintain homeostatic and metabolic integrity, and repair damage. Since growth depends on protein synthesis through ribosome biogenesis, the control of biosynthesis of ribosomes is necessarily a key element for control of growth. Nucleolin is a major nucleolar protein of exponentially growing eukaryotic cells, which is directly involved in the regulation of ribosome biogenesis and maturation. The highly conserved nucleolin contains three major domains through which it controls the organization of nucleolar chromatin, packaging of pre-RNA, rDNA transcription, and ribosome assembly. Numerous reports have implicated the involvement of nucleolin either directly or indirectly in the regulation of cell proliferation and growth, cytokinesis, replication, embryogenesis, and nucleogenesis. Nucleolin, an RNA binding protein, is also an autoantigen, a transcriptional repressor, and a switch region targeting factor. In addition, nucleolin exhibits autodegradation, DNA and RNA helicase activities, and DNA-dependent ATPase activity. An interesting aspect of nucleolin action is that it is a target for regulation by proteolysis, methylation, ADP-ribosylation, and phosphorylation by CKII, cdc2, PKC-xi, cyclic AMP-dependent protein kinase, and ecto-protein kinase. For these and other reasons, nucleolin is fundamental to the survival and proliferation of cells. Considerable progress has been made in recent years with the identification of new nucleolin binding proteins that may mediate these many nucleolin-dependent functions. Nucleolin also functions as a cell surface receptor, where it acts as a shuttling protein between cytoplasm and nucleus, and thus can even provide a mechanism for extracellular regulation of nuclear events. Exploration of the regulation of this multifaceted protein in a remarkable number of diverse functions is challenging.

Similar articles

• Nucleolin: a multifunctional major nucleolar phosphoprotein.

  Tuteja R, Tuteja N. Tuteja R, et al. Crit Rev Biochem Mol Biol. 1998;33(6):407-36. doi: 10.1080/10409239891204260. Crit Rev Biochem Mol Biol. 1998. PMID: 9918513 Review.

• New perspectives of physiological and pathological functions of nucleolin (NCL).

  Jia W, Yao Z, Zhao J, Guan Q, Gao L. Jia W, et al. Life Sci. 2017 Oct 1;186:1-10. doi: 10.1016/j.lfs.2017.07.025. Epub 2017 Jul 24. Life Sci. 2017. PMID: 28751161 Review.

• Nucleolar localization of aprataxin is dependent on interaction with nucleolin and on active ribosomal DNA transcription.

  Becherel OJ, Gueven N, Birrell GW, Schreiber V, Suraweera A, Jakob B, Taucher-Scholz G, Lavin MF. Becherel OJ, et al. Hum Mol Genet. 2006 Jul 15;15(14):2239-49. doi: 10.1093/hmg/ddl149. Epub 2006 Jun 15. Hum Mol Genet. 2006. PMID: 16777843

• Inactivation of nucleolin leads to nucleolar disruption, cell cycle arrest and defects in centrosome duplication.

  Ugrinova I, Monier K, Ivaldi C, Thiry M, Storck S, Mongelard F, Bouvet P. Ugrinova I, et al. BMC Mol Biol. 2007 Aug 10;8:66. doi: 10.1186/1471-2199-8-66. BMC Mol Biol. 2007. PMID: 17692122 Free PMC article.

• Structure and functions of nucleolin.

  Ginisty H, Sicard H, Roger B, Bouvet P. Ginisty H, et al. J Cell Sci. 1999 Mar;112 ( Pt 6):761-72. doi: 10.1242/jcs.112.6.761. J Cell Sci. 1999. PMID: 10036227 Review.

Cited by

• Human anti-nucleolin recombinant immunoagent for cancer therapy.

  Palmieri D, Richmond T, Piovan C, Sheetz T, Zanesi N, Troise F, James C, Wernicke D, Nyei F, Gordon TJ, Consiglio J, Salvatore F, Coppola V, Pichiorri F, De Lorenzo C, Croce CM. Palmieri D, et al. Proc Natl Acad Sci U S A. 2015 Jul 28;112(30):9418-23. doi: 10.1073/pnas.1507087112. Epub 2015 Jul 13. Proc Natl Acad Sci U S A. 2015. PMID: 26170308 Free PMC article.

• Cell surface nucleolin on developing muscle is a potential ligand for the axonal receptor protein tyrosine phosphatase-sigma.

  Alete DE, Weeks ME, Hovanession AG, Hawadle M, Stoker AW. Alete DE, et al. FEBS J. 2006 Oct;273(20):4668-81. doi: 10.1111/j.1742-4658.2006.05471.x. Epub 2006 Sep 21. FEBS J. 2006. PMID: 16995858 Free PMC article.

• Nucleolin: acharan sulfate-binding protein on the surface of cancer cells.

  Joo EJ, ten Dam GB, van Kuppevelt TH, Toida T, Linhardt RJ, Kim YS. Joo EJ, et al. Glycobiology. 2005 Jan;15(1):1-9. doi: 10.1093/glycob/cwh132. Epub 2004 Aug 25. Glycobiology. 2005. PMID: 15329357 Free PMC article.

• Nucleolin promotes angiogenesis and endothelial metabolism along the oncofetal axis in the human brain vasculature.

  Schwab M, de Trizio I, Ghobrial M, Shiu JY, Sürücü O, Girolamo F, Errede M, Yilmaz M, Haybaeck J, Moiraghi A, Monnier PP, Lawler SE, Greenfield JP, Radovanovic I, Frei K, Schlapbach R, Vogel V, Virgintino D, De Bock K, Wälchli T. Schwab M, et al. JCI Insight. 2023 Apr 24;8(8):e143071. doi: 10.1172/jci.insight.143071. JCI Insight. 2023. PMID: 36917178 Free PMC article.

• SLOW WALKER2, a NOC1/MAK21 homologue, is essential for coordinated cell cycle progression during female gametophyte development in Arabidopsis.

  Li N, Yuan L, Liu N, Shi D, Li X, Tang Z, Liu J, Sundaresan V, Yang WC. Li N, et al. Plant Physiol. 2009 Nov;151(3):1486-97. doi: 10.1104/pp.109.142414. Epub 2009 Sep 4. Plant Physiol. 2009. PMID: 19734265 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Ovid Technologies, Inc.

• Other Literature Sources

  • The Lens - Patent Citations Database

• Molecular Biology Databases

  • Mouse Genome Informatics (MGI)

• Miscellaneous

  • NCI CPTAC Assay Portal