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ARS Home » Pacific West Area » Albany, California » Plant Gene Expression Center » Research » Publications at this Location » Publication #136021
Title: A CYSTEINE-RICH EXTRACELLULAR PROTEIN, LAT52, INTERACTS WITH THE EXTRACVELLULAR DOMAIN OF THE POLLEN RECEPTOR KINASE LEPRK2

Author
item TANG, W - ARS/UCB PLNT GENE EXP CTR
item EZCURRA, INES - ARS/UCB PLNT GENE EXP CTR
item MUSCHIETTI, JORGE - ARS/UCB PLNT GENE EXP CTR
item McCormick, Sheila

Submitted to: The Plant Cell
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/19/2002
Publication Date: 9/1/2002
Citation: TANG, W., EZCURRA, I., MUSCHIETTI, J., MCCORMICK, S.M. A CYSTEINE-RICH EXTRACELLULAR PROTEIN, LAT52, INTERACTS WITH THE EXTRACVELLULAR DOMAIN OF THE POLLEN RECEPTOR KINASE LEPRK2. THE PLANT CELL. 2002. 14:2277-2287.

Interpretive Summary: Pollen germination and pollen tube growth require extracellular cues. Pollen receptor kinases might bind extracellular ligands and thereby mediate pollen germination and pollen tube growth. We identified numerous secreted or plasma membrane-bound candidate ligands. One of these, LAT52, was known to be essential during pollen hydration and forms a complex with LePRK2 in pollen. We propose that LAT52 might be a ligand for LePRK2.

Technical Abstract: Pollen germination and pollen tube growth are thought to require extracellular cues, but how these cues are perceived and transduced remains largely unknown. Pollen receptor kinases are plausible candidates for this role; they might bind extracellular ligands and thereby mediate cytoplasmic events required for pollen germination and pollen tube growth. To search for pollen-expressed ligands for pollen receptor kinases, we used the extracellular domains of three pollen-specific receptor kinases of tomato (LePRKl, LePRK2 or LePRK3) as baits in a yeast two-hybrid screen. We identified numerous secreted or plasma membrane-bound candidate ligands. One of these, the cysteine-rich protein LAT52, was already known to be essential during pollen hydration ation and pollen tube growth. We used in vivo co-immunoprecipitation to demonstrate LAT52 was capable of forming a complex with LePRK2 in pollen, and to show that the extracellular domain of LePRK2 was sufficient for the interaction. Soluble LAT52 can exist in different-sized forms, but only the larger form can interact with LePRK2. We propose that LAT52 might be a ligand for LePRK2.