Literature DB >> 1618898

Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA.

C Kambach1, I W Mattaj.   

Abstract

Nuclear transport of the U1 snRNP-specific protein U1A has been examined. U1A moves to the nucleus by an active process which is independent of interaction with U1 snRNA. Nuclear localization requires an unusually large sequence element situated between amino acids 94 and 204 of the protein. U1A transport is not unidirectional. The protein shuttles between nucleus and cytoplasm. At equilibrium, the concentration of the protein in the nucleus and cytoplasm is not, however, determined solely by transport rates, but can be perturbed by introducing RNA sequences that can specifically bind U1A in either the nuclear or cytoplasmic compartment. Thus, U1A represents a novel class of protein which shuttles between cytoplasm and nucleus and whose intracellular distribution can be altered by the number of free binding sites for the protein present in the cytoplasm or the nucleus.

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Year:  1992        PMID: 1618898      PMCID: PMC2289521          DOI: 10.1083/jcb.118.1.11

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  51 in total

Review 1.  Nuclear protein localization.

Authors:  J Garcia-Bustos; J Heitman; M N Hall
Journal:  Biochim Biophys Acta       Date:  1991-03-07

2.  Evidence for three distinct D proteins, which react differentially with anti-Sm autoantibodies, in the cores of the major snRNPs U1, U2, U4/U6 and U5.

Authors:  T Lehmeier; K Foulaki; R Lührmann
Journal:  Nucleic Acids Res       Date:  1990-11-25       Impact factor: 16.971

3.  Analysis of in vitro binding of U1-A protein mutants to U1 snRNA.

Authors:  W Boelens; D Scherly; E J Jansen; K Kolen; I W Mattaj; W J van Venrooij
Journal:  Nucleic Acids Res       Date:  1991-09-11       Impact factor: 16.971

4.  Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence.

Authors:  J Robbins; S M Dilworth; R A Laskey; C Dingwall
Journal:  Cell       Date:  1991-02-08       Impact factor: 41.582

Review 5.  The trimethyl-guanosine cap is a nuclear targeting signal for snRNPs.

Authors:  A L Lamond
Journal:  Trends Biochem Sci       Date:  1990-12       Impact factor: 13.807

Review 6.  Structure of spliceosomal snRNPs and their role in pre-mRNA splicing.

Authors:  R Lührmann; B Kastner; M Bach
Journal:  Biochim Biophys Acta       Date:  1990-11-30

7.  U2 snRNA sequences that bind U2-specific proteins are dispensable for the function of U2 snRNP in splicing.

Authors:  Z Q Pan; C Prives
Journal:  Genes Dev       Date:  1989-12       Impact factor: 11.361

8.  Microinjected U snRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways.

Authors:  N Michaud; D Goldfarb
Journal:  J Cell Biol       Date:  1992-02       Impact factor: 10.539

9.  Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope.

Authors:  R B Mandell; C M Feldherr
Journal:  J Cell Biol       Date:  1990-11       Impact factor: 10.539

10.  Diversity in the signals required for nuclear accumulation of U snRNPs and variety in the pathways of nuclear transport.

Authors:  U Fischer; E Darzynkiewicz; S M Tahara; N A Dathan; R Lührmann; I W Mattaj
Journal:  J Cell Biol       Date:  1991-05       Impact factor: 10.539

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  54 in total

1.  The carboxyl terminus of RNA helicase A contains a bidirectional nuclear transport domain.

Authors:  H Tang; D McDonald; T Middlesworth; T J Hope; F Wong-Staal
Journal:  Mol Cell Biol       Date:  1999-05       Impact factor: 4.272

2.  TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus.

Authors:  I C Braun; E Rohrbach; C Schmitt; E Izaurralde
Journal:  EMBO J       Date:  1999-04-01       Impact factor: 11.598

3.  Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry.

Authors:  P Ajuh; B Kuster; K Panov; J C Zomerdijk; M Mann; A I Lamond
Journal:  EMBO J       Date:  2000-12-01       Impact factor: 11.598

4.  Regulation of nuclear poly(A) addition controls the expression of immunoglobulin M secretory mRNA.

Authors:  C Phillips; S Jung; S I Gunderson
Journal:  EMBO J       Date:  2001-11-15       Impact factor: 11.598

5.  Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway.

Authors:  M D Koffa; J B Clements; E Izaurralde; S Wadd; S A Wilson; I W Mattaj; S Kuersten
Journal:  EMBO J       Date:  2001-10-15       Impact factor: 11.598

6.  The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5' splice sites.

Authors:  Patrik Förch; Oscar Puig; Concepción Martínez; Bertrand Séraphin; Juan Valcárcel
Journal:  EMBO J       Date:  2002-12-16       Impact factor: 11.598

7.  Use of fluorescent protein tags to study nuclear organization of the spliceosomal machinery in transiently transformed living plant cells.

Authors:  Zdravko J Lorković; Julia Hilscher; Andrea Barta
Journal:  Mol Biol Cell       Date:  2004-05-07       Impact factor: 4.138

8.  RNA length defines RNA export pathway.

Authors:  Kaoru Masuyama; Ichiro Taniguchi; Naoyuki Kataoka; Mutsuhito Ohno
Journal:  Genes Dev       Date:  2004-08-16       Impact factor: 11.361

Review 9.  The Cajal body: a meeting place for spliceosomal snRNPs in the nuclear maze.

Authors:  David Stanek; Karla M Neugebauer
Journal:  Chromosoma       Date:  2006-03-31       Impact factor: 4.316

10.  Non-snRNP U1A levels decrease during mammalian B-cell differentiation and release the IgM secretory poly(A) site from repression.

Authors:  Jianglin Ma; Samuel I Gunderson; Catherine Phillips
Journal:  RNA       Date:  2006-01       Impact factor: 4.942

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