Arginylation of β-actin regulates actin cytoskeleton and cell motility

Marina Karakozova; Marina Kozak; Catherine C L Wong; Aaron O. Bailey; John R. Yates; Alexander Mogilner; Henry Zebroski; Anna Kashina

doi:10.1126/science.1129344

Arginylation of β-actin regulates actin cytoskeleton and cell motility

Marina Karakozova, Marina Kozak, Catherine C L Wong, Aaron O. Bailey, John R. Yates, Alexander Mogilner, Henry Zebroski, Anna Kashina

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

Abstract

Posttranslational arginylation is critical for mouse embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are unknown. We found that β-actin was arginylated in vivo to regulate actin filament properties, β-actin localization, and lamella formation in motile cells. Arginylation of β-actin apparently represents a critical step in the actin N-terminal processing needed for actin functioning in vivo. Thus, posttranslational arginylation of a single protein target can regulate its intracellular function, inducing global changes on the cellular level, and may contribute to cardiovascular development and angiogenesis.

Original language	English (US)
Pages (from-to)	192-196
Number of pages	5
Journal	Science
Volume	313
Issue number	5784
DOIs	https://doi.org/10.1126/science.1129344
State	Published - Jul 14 2006

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title = "Arginylation of β-actin regulates actin cytoskeleton and cell motility",

abstract = "Posttranslational arginylation is critical for mouse embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are unknown. We found that β-actin was arginylated in vivo to regulate actin filament properties, β-actin localization, and lamella formation in motile cells. Arginylation of β-actin apparently represents a critical step in the actin N-terminal processing needed for actin functioning in vivo. Thus, posttranslational arginylation of a single protein target can regulate its intracellular function, inducing global changes on the cellular level, and may contribute to cardiovascular development and angiogenesis.",

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AU - Karakozova, Marina

AU - Kozak, Marina

AU - Wong, Catherine C L

AU - Bailey, Aaron O.

AU - Yates, John R.

AU - Mogilner, Alexander

AU - Zebroski, Henry

AU - Kashina, Anna

PY - 2006/7/14

Y1 - 2006/7/14

N2 - Posttranslational arginylation is critical for mouse embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are unknown. We found that β-actin was arginylated in vivo to regulate actin filament properties, β-actin localization, and lamella formation in motile cells. Arginylation of β-actin apparently represents a critical step in the actin N-terminal processing needed for actin functioning in vivo. Thus, posttranslational arginylation of a single protein target can regulate its intracellular function, inducing global changes on the cellular level, and may contribute to cardiovascular development and angiogenesis.

AB - Posttranslational arginylation is critical for mouse embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are unknown. We found that β-actin was arginylated in vivo to regulate actin filament properties, β-actin localization, and lamella formation in motile cells. Arginylation of β-actin apparently represents a critical step in the actin N-terminal processing needed for actin functioning in vivo. Thus, posttranslational arginylation of a single protein target can regulate its intracellular function, inducing global changes on the cellular level, and may contribute to cardiovascular development and angiogenesis.

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Arginylation of β-actin regulates actin cytoskeleton and cell motility

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