Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation.
Apoptosis-associated tyrosine kinase 1 (AATYK1), a novel serine/threonine kinase that is highly expressed in the brain, is involved in neurite extension and apoptosis of cerebellar granule neurons; however, its precise function remains unknown. In this study, we investigated the interaction of AATYK...
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doaj-6478341fda694b38972943531a2418682020-11-25T02:43:08ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-04-0154e1026010.1371/journal.pone.0010260Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation.Koji TsutsumiTetsuya TakanoRyo EndoMitsunori FukudaToshio OhshimaMineko TomomuraShin-ichi HisanagaApoptosis-associated tyrosine kinase 1 (AATYK1), a novel serine/threonine kinase that is highly expressed in the brain, is involved in neurite extension and apoptosis of cerebellar granule neurons; however, its precise function remains unknown. In this study, we investigated the interaction of AATYK1A with Cyclin-dependent kinase 5 (Cdk5)/p35, a proline-directed protein kinase that is predominantly expressed in neurons. AATYK1A bound to the p35 activation subunit of Cdk5 in cultured cells and in mouse brains and colocalized with p35 on endosomes in COS-7 cells. AATYK1A was phosphorylated at Ser34 by Cdk5/p35 in vitro, in cultured neurons and in mouse brain. In PC12D cells, Ser34 phosphorylation increased after treatment with nerve growth factor and phosphorylated AATYK1A accumulated in growth cones of PC12D cells. Ser34 phosphorylation suppressed the tyrosine phosphorylation of AATYK1A by Src family kinases. These results suggest a possibility that AATYK1A plays a role in early to recycling endosomes and its function is regulated by phosphorylation with Cdk5 or Src-family kinases.http://europepmc.org/articles/PMC2857886?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Koji Tsutsumi Tetsuya Takano Ryo Endo Mitsunori Fukuda Toshio Ohshima Mineko Tomomura Shin-ichi Hisanaga |
spellingShingle |
Koji Tsutsumi Tetsuya Takano Ryo Endo Mitsunori Fukuda Toshio Ohshima Mineko Tomomura Shin-ichi Hisanaga Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation. PLoS ONE |
author_facet |
Koji Tsutsumi Tetsuya Takano Ryo Endo Mitsunori Fukuda Toshio Ohshima Mineko Tomomura Shin-ichi Hisanaga |
author_sort |
Koji Tsutsumi |
title |
Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation. |
title_short |
Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation. |
title_full |
Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation. |
title_fullStr |
Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation. |
title_full_unstemmed |
Phosphorylation of AATYK1 by Cdk5 suppresses its tyrosine phosphorylation. |
title_sort |
phosphorylation of aatyk1 by cdk5 suppresses its tyrosine phosphorylation. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2010-04-01 |
description |
Apoptosis-associated tyrosine kinase 1 (AATYK1), a novel serine/threonine kinase that is highly expressed in the brain, is involved in neurite extension and apoptosis of cerebellar granule neurons; however, its precise function remains unknown. In this study, we investigated the interaction of AATYK1A with Cyclin-dependent kinase 5 (Cdk5)/p35, a proline-directed protein kinase that is predominantly expressed in neurons. AATYK1A bound to the p35 activation subunit of Cdk5 in cultured cells and in mouse brains and colocalized with p35 on endosomes in COS-7 cells. AATYK1A was phosphorylated at Ser34 by Cdk5/p35 in vitro, in cultured neurons and in mouse brain. In PC12D cells, Ser34 phosphorylation increased after treatment with nerve growth factor and phosphorylated AATYK1A accumulated in growth cones of PC12D cells. Ser34 phosphorylation suppressed the tyrosine phosphorylation of AATYK1A by Src family kinases. These results suggest a possibility that AATYK1A plays a role in early to recycling endosomes and its function is regulated by phosphorylation with Cdk5 or Src-family kinases. |
url |
http://europepmc.org/articles/PMC2857886?pdf=render |
work_keys_str_mv |
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