MAP Kinase PrMPK9-1 Contributes to the Self-Incompatibility Response

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MAP Kinase PrMPK9-1 Contributes to the Self-Incompatibility Response. / Chai, Lijun; Tudor, Richard L.; Poulter, Natalie S.; Wilkins, Katie A.; Eaves, Deborah J.; Franklin, F. Christopher H.; Franklin-tong, Vernonica E.

In: PLANT PHYSIOLOGY, Vol. 174, No. 2, 05.06.2017, p. 1226-1237.

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@article{48f78161c6fa46b2aa388f2f959d13a8,
title = "MAP Kinase PrMPK9-1 Contributes to the Self-Incompatibility Response",
abstract = "Mitogen-activated protein kinases (MAPKs) form important signaling modules for a variety of cellular responses in eukaryotic cells. In plants, MAPKs play key roles in growth and development as well as in immunity/stress responses. Pollen-pistil interactions are critical early events regulating pollination and fertilization and involve many signaling events. Self-incompatibility (SI) is an important mechanism to prevent self-fertilization and inbreeding in higher plants and also is known to utilize signaling to achieve incompatible pollen rejection. Although several pollen-expressed MAPKs exist, very little is known about their function. We previously identified a pollen-expressed MAPK (p56) from Papaver rhoeas that was rapidly activated during SI; several studies implicated its role in signaling to SI-induced programmed cell death involving a DEVDase. However, to date, the identity of the MAPK involved has been unknown. Here, we have identified and cloned a pollen-expressed P. rhoeas threonine-aspartate-tyrosine (TDY) MAPK, PrMPK9-1. Rather few data relating to the function of TDY MAPKs in plants currently exist. We provide evidence that PrMPK9-1 has a cell type-specific function, with a distinct role from AtMPK9. To our knowledge, this is the first study implicating a function for a TDY MAPK in pollen. We show that PrMPK9-1 corresponds to p56 and demonstrate that it is functionally involved in mediating SI in P. rhoeas pollen: PrMPK9-1 is a key regulator for SI in pollen and acts upstream of programmed cell death involving actin and activation of a DEVDase. Our study provides an important advance in elucidating functional roles for this class of MAPKs.",
author = "Lijun Chai and Tudor, {Richard L.} and Poulter, {Natalie S.} and Wilkins, {Katie A.} and Eaves, {Deborah J.} and Franklin, {F. Christopher H.} and Franklin-tong, {Vernonica E.}",
year = "2017",
month = jun,
day = "5",
doi = "10.1104/pp.17.00213",
language = "English",
volume = "174",
pages = "1226--1237",
journal = "PLANT PHYSIOLOGY",
issn = "0032-0889",
publisher = "American Society of Plant Biologists",
number = "2",

}

RIS

TY - JOUR

T1 - MAP Kinase PrMPK9-1 Contributes to the Self-Incompatibility Response

AU - Chai, Lijun

AU - Tudor, Richard L.

AU - Poulter, Natalie S.

AU - Wilkins, Katie A.

AU - Eaves, Deborah J.

AU - Franklin, F. Christopher H.

AU - Franklin-tong, Vernonica E.

PY - 2017/6/5

Y1 - 2017/6/5

N2 - Mitogen-activated protein kinases (MAPKs) form important signaling modules for a variety of cellular responses in eukaryotic cells. In plants, MAPKs play key roles in growth and development as well as in immunity/stress responses. Pollen-pistil interactions are critical early events regulating pollination and fertilization and involve many signaling events. Self-incompatibility (SI) is an important mechanism to prevent self-fertilization and inbreeding in higher plants and also is known to utilize signaling to achieve incompatible pollen rejection. Although several pollen-expressed MAPKs exist, very little is known about their function. We previously identified a pollen-expressed MAPK (p56) from Papaver rhoeas that was rapidly activated during SI; several studies implicated its role in signaling to SI-induced programmed cell death involving a DEVDase. However, to date, the identity of the MAPK involved has been unknown. Here, we have identified and cloned a pollen-expressed P. rhoeas threonine-aspartate-tyrosine (TDY) MAPK, PrMPK9-1. Rather few data relating to the function of TDY MAPKs in plants currently exist. We provide evidence that PrMPK9-1 has a cell type-specific function, with a distinct role from AtMPK9. To our knowledge, this is the first study implicating a function for a TDY MAPK in pollen. We show that PrMPK9-1 corresponds to p56 and demonstrate that it is functionally involved in mediating SI in P. rhoeas pollen: PrMPK9-1 is a key regulator for SI in pollen and acts upstream of programmed cell death involving actin and activation of a DEVDase. Our study provides an important advance in elucidating functional roles for this class of MAPKs.

AB - Mitogen-activated protein kinases (MAPKs) form important signaling modules for a variety of cellular responses in eukaryotic cells. In plants, MAPKs play key roles in growth and development as well as in immunity/stress responses. Pollen-pistil interactions are critical early events regulating pollination and fertilization and involve many signaling events. Self-incompatibility (SI) is an important mechanism to prevent self-fertilization and inbreeding in higher plants and also is known to utilize signaling to achieve incompatible pollen rejection. Although several pollen-expressed MAPKs exist, very little is known about their function. We previously identified a pollen-expressed MAPK (p56) from Papaver rhoeas that was rapidly activated during SI; several studies implicated its role in signaling to SI-induced programmed cell death involving a DEVDase. However, to date, the identity of the MAPK involved has been unknown. Here, we have identified and cloned a pollen-expressed P. rhoeas threonine-aspartate-tyrosine (TDY) MAPK, PrMPK9-1. Rather few data relating to the function of TDY MAPKs in plants currently exist. We provide evidence that PrMPK9-1 has a cell type-specific function, with a distinct role from AtMPK9. To our knowledge, this is the first study implicating a function for a TDY MAPK in pollen. We show that PrMPK9-1 corresponds to p56 and demonstrate that it is functionally involved in mediating SI in P. rhoeas pollen: PrMPK9-1 is a key regulator for SI in pollen and acts upstream of programmed cell death involving actin and activation of a DEVDase. Our study provides an important advance in elucidating functional roles for this class of MAPKs.

U2 - 10.1104/pp.17.00213

DO - 10.1104/pp.17.00213

M3 - Article

C2 - 28385731

VL - 174

SP - 1226

EP - 1237

JO - PLANT PHYSIOLOGY

JF - PLANT PHYSIOLOGY

SN - 0032-0889

IS - 2

ER -