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

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 (eS...

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Main Authors: Sushma Naithani, Thanat Chookajorn, Daniel R. Ripoll, June B. Nasrallah
Other Authors: Cornell University
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Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/25153
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spelling th-mahidol.251532018-08-24T09:18:18Z Structural modules for receptor dimerization in the S-locus receptor kinase extracellular domain Sushma Naithani Thanat Chookajorn Daniel R. Ripoll June B. Nasrallah Cornell University Mahidol University Multidisciplinary 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. © 2007 by The National Academy of Sciences of the USA. 2018-08-24T02:18:18Z 2018-08-24T02:18:18Z 2007-07-17 Article Proceedings of the National Academy of Sciences of the United States of America. Vol.104, No.29 (2007), 12211-12216 10.1073/pnas.0705186104 00278424 2-s2.0-34547503841 https://repository.li.mahidol.ac.th/handle/123456789/25153 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=34547503841&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Multidisciplinary
spellingShingle Multidisciplinary
Sushma Naithani
Thanat Chookajorn
Daniel R. Ripoll
June B. Nasrallah
Structural modules for receptor dimerization in the S-locus receptor kinase extracellular domain
description 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. © 2007 by The National Academy of Sciences of the USA.
author2 Cornell University
author_facet Cornell University
Sushma Naithani
Thanat Chookajorn
Daniel R. Ripoll
June B. Nasrallah
format Article
author Sushma Naithani
Thanat Chookajorn
Daniel R. Ripoll
June B. Nasrallah
author_sort Sushma Naithani
title Structural modules for receptor dimerization in the S-locus receptor kinase extracellular domain
title_short Structural modules for receptor dimerization in the S-locus receptor kinase extracellular domain
title_full Structural modules for receptor dimerization in the S-locus receptor kinase extracellular domain
title_fullStr Structural modules for receptor dimerization in the S-locus receptor kinase extracellular domain
title_full_unstemmed Structural modules for receptor dimerization in the S-locus receptor kinase extracellular domain
title_sort structural modules for receptor dimerization in the s-locus receptor kinase extracellular domain
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/25153
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