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Wall-associated kinase
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Wall-associated kinase
Wall-associated kinases (WAKs) are one of many classes of plant proteins known to serve as a medium between the extracellular matrix (ECM) and cytoplasm of cell walls. They are serine-threonine kinases that contain epidermal growth factor (EGF) repeats, a cytoplasmic kinase and are located in the cell walls. They provide a linkage between the inner and outer surroundings of cell walls. WAKs are under a group of receptor-like kinases (RLK) that are actively involved in sensory and signal transduction pathways especially in response to foreign attacks by pathogens and in cell development. On the other hand, pectins are an abundant group of complex carbohydrates present in the primary cell wall that play roles in cell growth and development, protection, plant structure and water holding capacity.
Cell wall associated kinases are receptor-like protein kinases, found in plant cell walls, that have the capability to transmit signals directly by their cytoplasmic kinase domains. They usually link the plasma membrane to the protein and carbohydrate that composed the cell wall. The receptor-like proteins contain a cytoplasmic serine threonine kinase and a less conserved region; bound to the cell wall and contains a series of epidermal growth factor repeats. WAKs are found in various plants and crops like rice, and maize. In plants genome like Arabidopsis, WAKs, are encoded by five highly similar genes clustered in a 30-kb locus, among them WAK1 & WAK2 are highly distributed. They are primarily involved in regulating plant cell wall functions including cell expansion, bind as well as response to pectins, pathogen response and also protects plants from detrimental effects.
Pectins are rich in galacturonic acids (OGs) and present in the middle lamellae in plant tissues where they provide strength, flexibility and adhesion between plant cells. Commercially and within the food industry, they are used as gels and stabilizers for desserts and juices. The role of WAKs in cell walls as pectin receptors is vital to a variety of functions involved with cell differentiation, form and host-pathogen relations.
The association of WAKs with The Plant Cell wall was first compromised by immunolocalization technique using antiserum where epitome of WAK are found to be tightly bound with cell wall fragments so that they can not be separated using detergent, however, WAKs could be released by boiling the walls with SDS, dithiothreitol (a strong thiol reductant), protoplasting enzymes or pectinase.
WAKs protein composed of five types of highly similar genes located tightly in a 30 kb clusters of Arabidopsis genome. Most of the WAKs are expressed throughout the plant whether WAK1, 2, 3 and 5 are expressed in green organs, WAK1 and 2 weakly expressed in flowers and siliques and WAK2 is also expressed in roots, however, WAK4 is only expressed in siliques. There are also 21 WAK like gene in Arabitopsis genome known as WAKLs which have a little sequence similarity with WAKs.
The Ara WAK and WAKL genes are distributed among all five chromosomes of Arabidopsis
WAK/WAKL gene family members in Arabidopsis were divided into four groups based on the pair-wise comparisons of their predicted protein sequences. WAK1 to WAK5 containing EGF-Ca2+ domain with an overlapping Asp/Asn hydroxylation site and an EGF-2 domain were placed in Group I. Both the EGF domains were predicted to be completely encoded by the second exon. Seven WAKL members that include WAKL1 to WAKL6 and WAKL22 were placed in Group II. In all these group II genes, the EGF-Ca2+ and EGF-2 domains are separated by a short gap of 15-18 aa and were reversed in order relative to group I. The EGF-Ca2+ domain is encoded by first exon and EGF-Ca2+ domain is encoded by second exon. No Asn/asp hydroxylation site was predicted.
Group III contains six members: WAKL9, WAKL10, WAKL11, WAKL13, WAKL17, and WAKL18. Their corresponding proteins all contain EGF-Ca2+ and EGF2 domains, and they are structurally similar to the Group II WAKLs. In WAKL13, the EGF-Ca2+ domain is degenerate. With the exception of WAKL17, all have degenerate EGF2 domains.
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Wall-associated kinase
Wall-associated kinases (WAKs) are one of many classes of plant proteins known to serve as a medium between the extracellular matrix (ECM) and cytoplasm of cell walls. They are serine-threonine kinases that contain epidermal growth factor (EGF) repeats, a cytoplasmic kinase and are located in the cell walls. They provide a linkage between the inner and outer surroundings of cell walls. WAKs are under a group of receptor-like kinases (RLK) that are actively involved in sensory and signal transduction pathways especially in response to foreign attacks by pathogens and in cell development. On the other hand, pectins are an abundant group of complex carbohydrates present in the primary cell wall that play roles in cell growth and development, protection, plant structure and water holding capacity.
Cell wall associated kinases are receptor-like protein kinases, found in plant cell walls, that have the capability to transmit signals directly by their cytoplasmic kinase domains. They usually link the plasma membrane to the protein and carbohydrate that composed the cell wall. The receptor-like proteins contain a cytoplasmic serine threonine kinase and a less conserved region; bound to the cell wall and contains a series of epidermal growth factor repeats. WAKs are found in various plants and crops like rice, and maize. In plants genome like Arabidopsis, WAKs, are encoded by five highly similar genes clustered in a 30-kb locus, among them WAK1 & WAK2 are highly distributed. They are primarily involved in regulating plant cell wall functions including cell expansion, bind as well as response to pectins, pathogen response and also protects plants from detrimental effects.
Pectins are rich in galacturonic acids (OGs) and present in the middle lamellae in plant tissues where they provide strength, flexibility and adhesion between plant cells. Commercially and within the food industry, they are used as gels and stabilizers for desserts and juices. The role of WAKs in cell walls as pectin receptors is vital to a variety of functions involved with cell differentiation, form and host-pathogen relations.
The association of WAKs with The Plant Cell wall was first compromised by immunolocalization technique using antiserum where epitome of WAK are found to be tightly bound with cell wall fragments so that they can not be separated using detergent, however, WAKs could be released by boiling the walls with SDS, dithiothreitol (a strong thiol reductant), protoplasting enzymes or pectinase.
WAKs protein composed of five types of highly similar genes located tightly in a 30 kb clusters of Arabidopsis genome. Most of the WAKs are expressed throughout the plant whether WAK1, 2, 3 and 5 are expressed in green organs, WAK1 and 2 weakly expressed in flowers and siliques and WAK2 is also expressed in roots, however, WAK4 is only expressed in siliques. There are also 21 WAK like gene in Arabitopsis genome known as WAKLs which have a little sequence similarity with WAKs.
The Ara WAK and WAKL genes are distributed among all five chromosomes of Arabidopsis
WAK/WAKL gene family members in Arabidopsis were divided into four groups based on the pair-wise comparisons of their predicted protein sequences. WAK1 to WAK5 containing EGF-Ca2+ domain with an overlapping Asp/Asn hydroxylation site and an EGF-2 domain were placed in Group I. Both the EGF domains were predicted to be completely encoded by the second exon. Seven WAKL members that include WAKL1 to WAKL6 and WAKL22 were placed in Group II. In all these group II genes, the EGF-Ca2+ and EGF-2 domains are separated by a short gap of 15-18 aa and were reversed in order relative to group I. The EGF-Ca2+ domain is encoded by first exon and EGF-Ca2+ domain is encoded by second exon. No Asn/asp hydroxylation site was predicted.
Group III contains six members: WAKL9, WAKL10, WAKL11, WAKL13, WAKL17, and WAKL18. Their corresponding proteins all contain EGF-Ca2+ and EGF2 domains, and they are structurally similar to the Group II WAKLs. In WAKL13, the EGF-Ca2+ domain is degenerate. With the exception of WAKL17, all have degenerate EGF2 domains.
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