Diacylglycerol and protein kinase D localization during T lymphocyte activation

Martin Spitaler; Elizabeth Emslie; C. David Wood; Doreen Cantrell

doi:10.1016/j.immuni.2006.02.013

Diacylglycerol and protein kinase D localization during T lymphocyte activation

Martin Spitaler
, Elizabeth Emslie
, C. David Wood
, Doreen Cantrell

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

99 Citations (Scopus)

Abstract

The serine kinase protein kinase D (PKD) has a cysteine-rich domain (CRD) that binds diacylglycerol (DAG) with high affinity. PKD is cytosolic in unstimulated T cells, but it rapidly polarizes to the immunological synapse in response to antigen/antigen presenting cells (APCs). PKD repositioning is determined by the accumulation of DAG at the immunological synapse and changes in DAG accessibility of the PKD-CRD. Unstimulated T cells are shown to have a uniform distribution of DAG at the plasma membrane, whereas after T cell activation, a gradient of DAG is created with a persistent focus of DAG at the center of the synapse. PKD is only transiently associated with the immune synapse, indicating a fine tuning of PKD responsiveness to DAG by additional regulatory mechanisms. These results reveal the immune synapse as a focal point for DAG and PKD as an immediate and dynamic DAG effector during T cell activation.

Original language	English
Pages (from-to)	535-546
Number of pages	12
Journal	Immunity
Volume	24
Issue number	5
DOIs	https://doi.org/10.1016/j.immuni.2006.02.013
Publication status	Published - 2006

Keywords

T lymphocytes
Protein kinase

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10.1016/j.immuni.2006.02.013

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title = "Diacylglycerol and protein kinase D localization during T lymphocyte activation",

abstract = "The serine kinase protein kinase D (PKD) has a cysteine-rich domain (CRD) that binds diacylglycerol (DAG) with high affinity. PKD is cytosolic in unstimulated T cells, but it rapidly polarizes to the immunological synapse in response to antigen/antigen presenting cells (APCs). PKD repositioning is determined by the accumulation of DAG at the immunological synapse and changes in DAG accessibility of the PKD-CRD. Unstimulated T cells are shown to have a uniform distribution of DAG at the plasma membrane, whereas after T cell activation, a gradient of DAG is created with a persistent focus of DAG at the center of the synapse. PKD is only transiently associated with the immune synapse, indicating a fine tuning of PKD responsiveness to DAG by additional regulatory mechanisms. These results reveal the immune synapse as a focal point for DAG and PKD as an immediate and dynamic DAG effector during T cell activation.",

keywords = "T lymphocytes, Protein kinase",

author = "Martin Spitaler and Elizabeth Emslie and Wood, \{C. David\} and Doreen Cantrell",

note = "dc.publisher: Elsevier ",

year = "2006",

doi = "10.1016/j.immuni.2006.02.013",

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journal = "Immunity",

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T1 - Diacylglycerol and protein kinase D localization during T lymphocyte activation

AU - Spitaler, Martin

AU - Emslie, Elizabeth

AU - Wood, C. David

AU - Cantrell, Doreen

N1 - dc.publisher: Elsevier

PY - 2006

Y1 - 2006

N2 - The serine kinase protein kinase D (PKD) has a cysteine-rich domain (CRD) that binds diacylglycerol (DAG) with high affinity. PKD is cytosolic in unstimulated T cells, but it rapidly polarizes to the immunological synapse in response to antigen/antigen presenting cells (APCs). PKD repositioning is determined by the accumulation of DAG at the immunological synapse and changes in DAG accessibility of the PKD-CRD. Unstimulated T cells are shown to have a uniform distribution of DAG at the plasma membrane, whereas after T cell activation, a gradient of DAG is created with a persistent focus of DAG at the center of the synapse. PKD is only transiently associated with the immune synapse, indicating a fine tuning of PKD responsiveness to DAG by additional regulatory mechanisms. These results reveal the immune synapse as a focal point for DAG and PKD as an immediate and dynamic DAG effector during T cell activation.

AB - The serine kinase protein kinase D (PKD) has a cysteine-rich domain (CRD) that binds diacylglycerol (DAG) with high affinity. PKD is cytosolic in unstimulated T cells, but it rapidly polarizes to the immunological synapse in response to antigen/antigen presenting cells (APCs). PKD repositioning is determined by the accumulation of DAG at the immunological synapse and changes in DAG accessibility of the PKD-CRD. Unstimulated T cells are shown to have a uniform distribution of DAG at the plasma membrane, whereas after T cell activation, a gradient of DAG is created with a persistent focus of DAG at the center of the synapse. PKD is only transiently associated with the immune synapse, indicating a fine tuning of PKD responsiveness to DAG by additional regulatory mechanisms. These results reveal the immune synapse as a focal point for DAG and PKD as an immediate and dynamic DAG effector during T cell activation.

KW - T lymphocytes

KW - Protein kinase

U2 - 10.1016/j.immuni.2006.02.013

DO - 10.1016/j.immuni.2006.02.013

M3 - Article

C2 - 16713972

SN - 1074-7613

VL - 24

SP - 535

EP - 546

JO - Immunity

JF - Immunity

IS - 5

ER -

Diacylglycerol and protein kinase D localization during T lymphocyte activation

Abstract

Keywords

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