南方科技大学知识苑(SUSTech KC): pH modulates interaction of 14-3-3 proteins with pollen plasma membrane H+ ATPases independently from phosphorylation

题名	pH modulates interaction of 14-3-3 proteins with pollen plasma membrane H+ ATPases independently from phosphorylation
作者	Pertl-Obermeyer, Heidi 1,2; Gimeno, Ana 1; Kuchler, Verena 1; Servili, Evrim 1,4; Huang, Shuai1,5 ; Fang, Han 1,6; Lang, Veronika 1,7; Sydow, Katharina 1; Poeckl, Magdalena 1; Schulze, Waltraud X.3; Obermeyer, Gerhard 1
通讯作者	Obermeyer, Gerhard
发表日期	2022
DOI	10.1093/jxb/erab387
发表期刊	JOURNAL OF EXPERIMENTAL BOTANY 影响因子和分区
ISSN	0022-0957
EISSN	1460-2431
卷号	73 期号:1
摘要	Pollen grains transport the sperm cells through the style tissue via a fast-growing pollen tube to the ovaries where fertilization takes place. Pollen tube growth requires a precisely regulated network of cellular as well as molecular events including the activity of the plasma membrane H+ ATPase, which is known to be regulated by reversible protein phosphorylation and subsequent binding of 14-3-3 isoforms. Immunodetection of the phosphorylated penultimate threonine residue of the pollen plasma membrane H+ ATPase (LilHA1) of Lilium longiflorum pollen revealed a sudden increase in phosphorylation with the start of pollen tube growth. In addition to phosphorylation, pH modulated the binding of 14-3-3 isoforms to the regulatory domain of the H+ ATPase, whereas metabolic components had only small effects on 14-3-3 binding, as tested with in vitro assays using recombinant 14-3-3 isoforms and phosphomimicking substitutions of the threonine residue. Consequently, local H+ influxes and effluxes as well as pH gradients in the pollen tube tip are generated by localized regulation of the H+ ATPase activity rather than by heterogeneous localized distribution in the plasma membrane.
关键词	14-3-3 protein cytosolic pH phosphorylation plasma membrane H+-ATPase pollen protein-protein interaction tip growth
相关链接	[来源记录]
收录类别	SCI
语种	英语
学校署名	其他
资助项目	Austrian Research Fund (FWF)["P21298","P29626"]
WOS研究方向	Plant Sciences
WOS类目	Plant Sciences
WOS记录号	WOS:000747681600015
出版者	OXFORD UNIV PRESS
ESI学科分类	PLANT & ANIMAL SCIENCE
来源库	Web of Science
引用统计	被引频次[WOS]：7
成果类型	期刊论文
条目标识符	http://sustech.caswiz.com/handle/2SGJ60CL/273541
专题	南方科技大学生命科学学院生命科学学院_生物系
作者单位	1.Univ Salzburg, Dept Biosci, Membrane Biophys, Billrothstr 11, A-5020 Salzburg, Austria 2.Univ Salzburg, Dept Chem & Phys Mat, MorphoPhys, Jakob Haringer Str 2a, A-5020 Salzburg, Austria 3.Univ Hohenheim, Plant Syst Biol, Garbenstr 30, D-70599 Stuttgart, Germany 4.Univ Louvain, Inst Rech Expt & Clin, Ave Hippocrate 57, B-1200 Woluwe St Lambert, Belgium 5.Southern Univ Sci & Technol, Shenzhen 518055, Peoples R China 6.Paracelsus Med Univ, Spinal Chord Injury & Tissue Regenerat Ctr, Strubergasse 22, A-5020 Salzburg, Austria 7.STRATEC GmbH, Sonystr 20, A-5081 Anif, Austria
推荐引用方式 GB/T 7714	Pertl-Obermeyer, Heidi,Gimeno, Ana,Kuchler, Verena,et al. pH modulates interaction of 14-3-3 proteins with pollen plasma membrane H+ ATPases independently from phosphorylation[J]. JOURNAL OF EXPERIMENTAL BOTANY,2022,73(1).
APA	Pertl-Obermeyer, Heidi.,Gimeno, Ana.,Kuchler, Verena.,Servili, Evrim.,Huang, Shuai.,...&Obermeyer, Gerhard.(2022).pH modulates interaction of 14-3-3 proteins with pollen plasma membrane H+ ATPases independently from phosphorylation.JOURNAL OF EXPERIMENTAL BOTANY,73(1).
MLA	Pertl-Obermeyer, Heidi,et al."pH modulates interaction of 14-3-3 proteins with pollen plasma membrane H+ ATPases independently from phosphorylation".JOURNAL OF EXPERIMENTAL BOTANY 73.1(2022).