A Cysteine-Rich Extracellular Protein, LAT52, Interacts with the Extracellular Domain of the Pollen Receptor Kinase LePRK2[W]

Tang, Weihua; Ezcurra, Inés; Muschietti, Jorge; McCormick, Sheila

doi:10.1105/tpc.003103

Cited by 197 publications

(168 citation statements)

References 38 publications

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“…One pollen-specific, Cysrich protein, LATE ANTHER TOMATO52 (LAT52), interacts in vivo with LePRK2; LAT52 is essential for pollen hydration and germination in vitro and for normal tube growth in vivo. This finding suggests that LAT52 and LePRK2 are members of an autocrine signaling cascade that may regulate and maintain pollen tube growth (Tang et al, 2002).…”

Section: Pollen Tube Invasion: Growing Into the Stigmamentioning

confidence: 94%

Pollen and Stigma Structure and Function: The Role of Diversity in Pollination

Edlund

Swanson

Preuss

2004

THE PLANT CELL ONLINE

492

431

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Section: Pollen Tube Invasion: Growing Into the Stigmamentioning

confidence: 94%

Pollen and Stigma Structure and Function: The Role of Diversity in Pollination

Edlund

Swanson

Preuss

2004

THE PLANT CELL ONLINE

492

431

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“…For this analysis, we used the yeast twohybrid system because, unlike our application of yeast surface display, this system can provide information on the strength of interactions (23), because the expression of three reporters, ADE2, HIS3, and LacZ, may be monitored by assessing the extent of cell growth on selective media under different stringency conditions and by measuring ␤-galactosidase activity (see Methods). Furthermore, this system has been particularly useful for investigating the role of individual domains or combination of domains in intermolecular interactions (24,25), and it is increasingly being used to investigate interactions between extracellular proteins (26)(27)(28).…”

Section: Identification Of Ligand-independent Dimerization Domains Inmentioning

confidence: 99%

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

Naithani¹,

Chookajorn²,

Ripoll

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

109

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The highly polymorphic S-locus receptor kinase (SRK) is the stigma determinant of specificity in the self-incompatibility response of the Brassicaceae. SRK spans the plasma membrane of stigma epidermal cells, and it is activated in an allele-specific manner on binding of its extracellular region (eSRK) to its cognate pollen coat-localized S-locus cysteine-rich (SCR) ligand. SRK, like several other receptor kinases, forms dimers in the absence of ligand. To identify domains in SRK that mediate ligand-independent dimerization, we assayed eSRK for self-interaction in yeast. We show that SRK dimerization is mediated by two regions in eSRK, primarily by a C-terminal region inferred by homology modeling/fold recognition techniques to assume a PAN APPLE-like structure, and secondarily by a region containing a signature sequence of the S-domain gene family, which might assume an EGF-like structure. We also show that eSRK exhibits a marked preference for homodimerization over heterodimerization with other eSRK variants and that this preference is mediated by a small, highly variable region within the PAN APPLE domain. Thus, the extensive polymorphism exhibited by the eSRK not only determines differential affinity toward the SCR ligand, as has been assumed thus far, but also underlies a previously unrecognized allelic specificity in SRK dimerization. We propose that preference for SRK homodimerization explains the codominance exhibited by a majority of SRKs in the typically heterozygous stigmas of self-incompatible plants, whereas an increased propensity for heterodimerization combined with reduced affinity of heterodimers for cognate SCRs might underlie the dominant-recessive or mutual weakening relationships exhibited by some SRK allelic pairs.self-incompatibility ͉ ligand-independent receptor dimerization ͉ yeast two-hybrid T he S-locus receptor kinase (SRK) is a single-pass integral plasma membrane protein of the stigma epidermis that functions in the recognition and rejection of self-related pollen in self-incompatible members of the Brassicaceae (reviewed in refs. 1 and 2). The SRK receptor and its pollen-coat localized ligand, the S-locus cysteine-rich protein (SCR) (1), also designated SP-11 (2), are encoded by tightly linked and highly polymorphic genes within the S-locus haplotype. Specificity in the self-incompatibility response derives from allele-specific SRK-SCR interaction (3, 4). On self-pollination, the binding of SCR to the extracellular domain of its cognate SRK activates the receptor and triggers an intracellular signaling cascade that leads to arrest of ''self'' pollen tubes. In contrast, pollen tube growth in cross-pollinations proceeds unimpeded because ''nonself'' SCR cannot bind SRK. In view of this high degree of specificity in the affinity of SRK for its SCR ligand, the extensive polymorphisms exhibited by the SRK extracellular region (eSRK) have heretofore been considered in the context of specificity in the SRK-SCR interaction.The eSRK does more than interact with SCR, however. SRK forms oligo...

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“…LePRK1 and LePRK2 in tomato pollen bind stably with each other and dissociate when exposed to the pistil extracts (Wengier et al, 2003). The pollen-derived peptide ligand LAT52 is a cysteine-rich peptide (CRP) with four cysteines and binds the extracellular domain of LePRK2 before pollination, and this binding is replaced by the stigma-derived LeSTIG1 (stigma-specific protein 1) (Tang et al, 2002. In petunia, the pollen cell wall located SHY binds the extracellular domain of PRK2, and likely performs a similar role as LAT52.…”

Section: Rlks Mediate Pollen Tube Growth In Pistilmentioning

confidence: 99%

RLKs orchestrate the signaling in plant male-female interaction

Yang

2016

Sci. China Life Sci.

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Different from animals, sessile plants are equipped with a large receptor-like kinase (RLK) superfamily. RLKs are a family of single trans-membrane proteins with divergent N-terminal extracellular domains capped by a signal peptide and C-terminal intracellular kinase. Researches in the last two decades have uncovered an increasing number of RLKs that regulate plant development, stress response and sexual reproduction, highlighting a dominant role of RLK signaling in cell-to-cell communications. Sexual reproduction in flowering plants is featured by interactions between the male gametophyte and the female tissues to facilitate sperm delivery and fertilization. Emerging evidences suggest that RLKs regulate almost every aspect of plant reproductive process, especially during pollination. Therefore, in this review we will focus mainly on the function and signaling of RLKs in plant male-female interaction and discuss the future prospects on these topics. RLK, signaling, plant reproduction, pollen tube, female gametophyte, male-female interaction, pollen tube growth and guidance, pollen tube reception Citation:Li, H., and Yang, W.C. (2016). RLKs orchestrate the signaling in plant male-female interaction. Sci China Life Sci 59, 867 -877.

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A Cysteine-Rich Extracellular Protein, LAT52, Interacts with the Extracellular Domain of the Pollen Receptor Kinase LePRK2[W]

Cited by 197 publications

References 38 publications

Pollen and Stigma Structure and Function: The Role of Diversity in Pollination

Pollen and Stigma Structure and Function: The Role of Diversity in Pollination

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

RLKs orchestrate the signaling in plant male-female interaction

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