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Literature DB >> 16794040

Arginylation of beta-actin regulates actin cytoskeleton and cell motility.

Marina Karakozova¹, Marina Kozak, Catherine C L Wong, Aaron O Bailey, John R Yates, Alexander Mogilner, Henry Zebroski, Anna Kashina.

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 beta-actin was arginylated in vivo to regulate actin filament properties, beta-actin localization, and lamella formation in motile cells. Arginylation of beta-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.

Entities: Gene Species

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Year: 2006 PMID： 16794040 DOI： 10.1126/science.1129344

Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728

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Cited

117 in total

1. Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.

Authors: Junling Wang; Xuemei Han; Sougata Saha; Tao Xu; Reena Rai; Fangliang Zhang; Yuri I Wolf; Alexey Wolfson; John R Yates; Anna Kashina
Journal: Chem Biol Date: 2011-01-28

Review 2. The N-end rule pathway: emerging functions and molecular principles of substrate recognition.

Authors: Shashikanth M Sriram; Bo Yeon Kim; Yong Tae Kwon
Journal: Nat Rev Mol Cell Biol Date: 2011-10-21 Impact factor: 94.444

Review 3. Nuclear actin and myosins: life without filaments.

Authors: Primal de Lanerolle; Leonid Serebryannyy
Journal: Nat Cell Biol Date: 2011-11-02 Impact factor: 28.824

4. The C-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (BRCA1) is degraded by the N-end rule pathway.

Authors: Zhizhong Xu; Roshani Payoe; Richard P Fahlman
Journal: J Biol Chem Date: 2012-01-18 Impact factor: 5.157

Review 5. Understanding neuronal connectivity through the post-transcriptional toolkit.

Authors: Carlos M Loya; David Van Vactor; Tudor A Fulga
Journal: Genes Dev Date: 2010-04-01 Impact factor: 11.361

6. tRNA^Arg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.

Authors: Irem Avcilar-Kucukgoze; Howard Gamper; Christine Polte; Zoya Ignatova; Ralph Kraetzner; Michael Shtutman; Ya-Ming Hou; Dawei W Dong; Anna Kashina
Journal: Cell Chem Biol Date: 2020-06-16 Impact factor: 8.116

7. Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis.

Authors: Sougata Saha; Junling Wang; Brian Buckley; Qingqing Wang; Brenda Lilly; Mikhail Chernov; Anna Kashina
Journal: Biochem Pharmacol Date: 2012-01-18 Impact factor: 5.858

Arginylation of beta-actin regulates actin cytoskeleton and cell motility.

1. Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.

Review 2. The N-end rule pathway: emerging functions and molecular principles of substrate recognition.

Review 3. Nuclear actin and myosins: life without filaments.

4. The C-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (BRCA1) is degraded by the N-end rule pathway.

Review 5. Understanding neuronal connectivity through the post-transcriptional toolkit.

6. tRNA^Arg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.

7. Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis.

Review 8. Local translation and directional steering in axons.

9. Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo.

Review 10. tRNAs: cellular barcodes for amino acids.

Arginylation of beta-actin regulates actin cytoskeleton and cell motility.

1. Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.

Review 2. The N-end rule pathway: emerging functions and molecular principles of substrate recognition.

Review 3. Nuclear actin and myosins: life without filaments.

4. The C-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (BRCA1) is degraded by the N-end rule pathway.

Review 5. Understanding neuronal connectivity through the post-transcriptional toolkit.

6. tRNAArg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.

7. Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis.

Review 8. Local translation and directional steering in axons.

9. Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo.

Review 10. tRNAs: cellular barcodes for amino acids.

6. tRNA^Arg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.