Unrip is a component of SMN complexes active in snRNP assembly

Claudia Carissimi; Jennifer Baccon; Marco Straccia; Pieranna Chiarella; Alessio Maiolica; Alan Sawyer; Juri Rappsilber; Livio Pellizzoni

doi:10.1016/j.febslet.2005.03.034

Unrip is a component of SMN complexes active in snRNP assembly

Claudia Carissimi, Jennifer Baccon, Marco Straccia, Pieranna Chiarella, Alessio Maiolica, Alan Sawyer, Juri Rappsilber, Livio Pellizzoni

Department of Pathology and Laboratory Medicine

Research output: Contribution to journal › Article › peer-review

67 Scopus citations

Abstract

A macromolecular complex containing survival of motor neurons (SMN), the spinal muscular atrophy protein, and Gemin2-7 interacts with Sm proteins and snRNAs to carry out the assembly of these components into spliceosomal small nuclear ribonucleoproteins (snRNPs). Here we report the characterization of unr-interacting protein (unrip), a GH-WD protein of unknown function, as a component of the SMN complex that interacts directly with Gemin6 and Gemin7. Unrip also binds a subset of Sm proteins, and unrip-containing SMN complexes are necessary and sufficient to mediate the assembly of spliceosomal snRNPs. These results demonstrate that unrip functions in the pathway of snRNP biogenesis and is a marker of cellular SMN complexes active in snRNP assembly.

Original language	English (US)
Pages (from-to)	2348-2354
Number of pages	7
Journal	FEBS Letters
Volume	579
Issue number	11
DOIs	https://doi.org/10.1016/j.febslet.2005.03.034
State	Published - Apr 25 2005

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/j.febslet.2005.03.034

Cite this

@article{9db7d2ceb77645e18828667c0d5f7ade,

title = "Unrip is a component of SMN complexes active in snRNP assembly",

abstract = "A macromolecular complex containing survival of motor neurons (SMN), the spinal muscular atrophy protein, and Gemin2-7 interacts with Sm proteins and snRNAs to carry out the assembly of these components into spliceosomal small nuclear ribonucleoproteins (snRNPs). Here we report the characterization of unr-interacting protein (unrip), a GH-WD protein of unknown function, as a component of the SMN complex that interacts directly with Gemin6 and Gemin7. Unrip also binds a subset of Sm proteins, and unrip-containing SMN complexes are necessary and sufficient to mediate the assembly of spliceosomal snRNPs. These results demonstrate that unrip functions in the pathway of snRNP biogenesis and is a marker of cellular SMN complexes active in snRNP assembly.",

author = "Claudia Carissimi and Jennifer Baccon and Marco Straccia and Pieranna Chiarella and Alessio Maiolica and Alan Sawyer and Juri Rappsilber and Livio Pellizzoni",

year = "2005",

month = apr,

day = "25",

doi = "10.1016/j.febslet.2005.03.034",

language = "English (US)",

volume = "579",

pages = "2348--2354",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "11",

}

TY - JOUR

T1 - Unrip is a component of SMN complexes active in snRNP assembly

AU - Carissimi, Claudia

AU - Baccon, Jennifer

AU - Straccia, Marco

AU - Chiarella, Pieranna

AU - Maiolica, Alessio

AU - Sawyer, Alan

AU - Rappsilber, Juri

AU - Pellizzoni, Livio

PY - 2005/4/25

Y1 - 2005/4/25

N2 - A macromolecular complex containing survival of motor neurons (SMN), the spinal muscular atrophy protein, and Gemin2-7 interacts with Sm proteins and snRNAs to carry out the assembly of these components into spliceosomal small nuclear ribonucleoproteins (snRNPs). Here we report the characterization of unr-interacting protein (unrip), a GH-WD protein of unknown function, as a component of the SMN complex that interacts directly with Gemin6 and Gemin7. Unrip also binds a subset of Sm proteins, and unrip-containing SMN complexes are necessary and sufficient to mediate the assembly of spliceosomal snRNPs. These results demonstrate that unrip functions in the pathway of snRNP biogenesis and is a marker of cellular SMN complexes active in snRNP assembly.

AB - A macromolecular complex containing survival of motor neurons (SMN), the spinal muscular atrophy protein, and Gemin2-7 interacts with Sm proteins and snRNAs to carry out the assembly of these components into spliceosomal small nuclear ribonucleoproteins (snRNPs). Here we report the characterization of unr-interacting protein (unrip), a GH-WD protein of unknown function, as a component of the SMN complex that interacts directly with Gemin6 and Gemin7. Unrip also binds a subset of Sm proteins, and unrip-containing SMN complexes are necessary and sufficient to mediate the assembly of spliceosomal snRNPs. These results demonstrate that unrip functions in the pathway of snRNP biogenesis and is a marker of cellular SMN complexes active in snRNP assembly.

UR - http://www.scopus.com/inward/record.url?scp=17644393497&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=17644393497&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2005.03.034

DO - 10.1016/j.febslet.2005.03.034

M3 - Article

C2 - 15848170

AN - SCOPUS:17644393497

SN - 0014-5793

VL - 579

SP - 2348

EP - 2354

JO - FEBS Letters

JF - FEBS Letters

IS - 11

ER -

Unrip is a component of SMN complexes active in snRNP assembly

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this