Dephosphorylation shows SR proteins the way out

Scott A. Tenenbaum; Julio Aguirre-Ghiso

doi:10.1016/j.molcel.2005.11.005

Dephosphorylation shows SR proteins the way out

Scott A. Tenenbaum, Julio Aguirre-Ghiso

Research output: Contribution to journal › Short survey › peer-review

13 Scopus citations

Abstract

To address the role of the RS domain in shuttling and how it is differentially required for constitutive and alternative splicing, Lin et al. (2005 [in the November 11 issue of Molecular Cell]) employ an elegant somatic complementation system to reveal a novel phosphorylation-dependent mechanism regulating distinct recycling pathways for SR proteins during mRNP maturation.

Original language	English (US)
Pages (from-to)	499-501
Number of pages	3
Journal	Molecular Cell
Volume	20
Issue number	4
DOIs	https://doi.org/10.1016/j.molcel.2005.11.005
State	Published - Nov 23 2005
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2005.11.005

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title = "Dephosphorylation shows SR proteins the way out",

abstract = "To address the role of the RS domain in shuttling and how it is differentially required for constitutive and alternative splicing, Lin et al. (2005 [in the November 11 issue of Molecular Cell]) employ an elegant somatic complementation system to reveal a novel phosphorylation-dependent mechanism regulating distinct recycling pathways for SR proteins during mRNP maturation.",

author = "Tenenbaum, {Scott A.} and Julio Aguirre-Ghiso",

year = "2005",

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doi = "10.1016/j.molcel.2005.11.005",

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journal = "Molecular Cell",

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T1 - Dephosphorylation shows SR proteins the way out

AU - Tenenbaum, Scott A.

AU - Aguirre-Ghiso, Julio

PY - 2005/11/23

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N2 - To address the role of the RS domain in shuttling and how it is differentially required for constitutive and alternative splicing, Lin et al. (2005 [in the November 11 issue of Molecular Cell]) employ an elegant somatic complementation system to reveal a novel phosphorylation-dependent mechanism regulating distinct recycling pathways for SR proteins during mRNP maturation.

AB - To address the role of the RS domain in shuttling and how it is differentially required for constitutive and alternative splicing, Lin et al. (2005 [in the November 11 issue of Molecular Cell]) employ an elegant somatic complementation system to reveal a novel phosphorylation-dependent mechanism regulating distinct recycling pathways for SR proteins during mRNP maturation.

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U2 - 10.1016/j.molcel.2005.11.005

DO - 10.1016/j.molcel.2005.11.005

M3 - Short survey

C2 - 16307914

AN - SCOPUS:27944504368

SN - 1097-2765

VL - 20

SP - 499

EP - 501

JO - Molecular Cell

JF - Molecular Cell

IS - 4

ER -

Dephosphorylation shows SR proteins the way out

Abstract

ASJC Scopus subject areas

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