Literature DB >> 11152955

14-3-3 proteins: regulation of subcellular localization by molecular interference.

A J Muslin1, H Xing.   

Abstract

14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic, and nutrient-sensing pathways. 14-3-3 proteins act by binding to partner proteins, and this binding often leads to the altered subcellular localization of the partner. 14-3-3 proteins promote the cytoplasmic localization of many binding partners, including the pro-apoptotic protein BAD and the cell cycle regulatory phosphatase Cdc25C, but they can also promote the nuclear localization of other partners, such as the catalytic subunit of telomerase (TERT). In some cases, 14-3-3 binding has no effect on the subcellular localization of a partner. 14-3-3 may affect the localization of a protein by interfering with the function of a nearby targeting sequence, such as a nuclear localization sequence (NLS) or a nuclear export sequence (NES), on the binding partner.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 11152955     DOI: 10.1016/s0898-6568(00)00131-5

Source DB:  PubMed          Journal:  Cell Signal        ISSN: 0898-6568            Impact factor:   4.315


  132 in total

Review 1.  Transport into and out of the nucleus.

Authors:  I G Macara
Journal:  Microbiol Mol Biol Rev       Date:  2001-12       Impact factor: 11.056

2.  Nuclear localization of CBF1 is regulated by interactions with the SMRT corepressor complex.

Authors:  S Zhou; S D Hayward
Journal:  Mol Cell Biol       Date:  2001-09       Impact factor: 4.272

3.  RGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domain.

Authors:  Jiaxin Niu; Astrid Scheschonka; Kirk M Druey; Amanda Davis; Eleanor Reed; Vladimir Kolenko; Richard Bodnar; Tatyana Voyno-Yasenetskaya; Xiaoping Du; John Kehrl; Nickolai O Dulin
Journal:  Biochem J       Date:  2002-08-01       Impact factor: 3.857

4.  Caspase cleavage of MST1 promotes nuclear translocation and chromatin condensation.

Authors:  S Ura; N Masuyama; J D Graves; Y Gotoh
Journal:  Proc Natl Acad Sci U S A       Date:  2001-08-21       Impact factor: 11.205

Review 5.  Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity.

Authors:  Paul C Sehnke; Justin M DeLille; Robert J Ferl
Journal:  Plant Cell       Date:  2002       Impact factor: 11.277

6.  Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3.

Authors:  Sindhu Rajan; Regina Preisig-Müller; Erhard Wischmeyer; Ralf Nehring; Peter J Hanley; Vijay Renigunta; Boris Musset; Günter Schlichthörl; Christian Derst; Andreas Karschin; Jürgen Daut
Journal:  J Physiol       Date:  2002-11-15       Impact factor: 5.182

7.  14-3-3 antagonizes Ras-mediated Raf-1 recruitment to the plasma membrane to maintain signaling fidelity.

Authors:  Yvonne Light; Hugh Paterson; Richard Marais
Journal:  Mol Cell Biol       Date:  2002-07       Impact factor: 4.272

8.  ERF nuclear shuttling, a continuous monitor of Erk activity that links it to cell cycle progression.

Authors:  Lionel Le Gallic; Laura Virgilio; Philip Cohen; Benoit Biteau; George Mavrothalassitis
Journal:  Mol Cell Biol       Date:  2004-02       Impact factor: 4.272

Review 9.  Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.

Authors:  Alastair Aitken
Journal:  Plant Mol Biol       Date:  2002-12       Impact factor: 4.076

Review 10.  14-3-3 proteins and the response to abiotic and biotic stress.

Authors:  Michael R Roberts; Julio Salinas; David B Collinge
Journal:  Plant Mol Biol       Date:  2002-12       Impact factor: 4.076

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.