A receptor-like cytoplasmic kinase PCRK2 undergoes ubiquitination and proteasomal degradation
Receptor-like cytoplasmic kinase (RLCK) subfamily VII members are involved in diverse biological processes, like reproduction, immunity, growth and development. Ubiquitination and proteasomal degradation of a RLCK VII member, BOTRYTIS-INDUCED KINASE1 (BIK1) play important roles in regulating immune...
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Veröffentlicht in: | Biochemical and biophysical research communications 2022-01, Vol.587, p.113-118 |
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description | Receptor-like cytoplasmic kinase (RLCK) subfamily VII members are involved in diverse biological processes, like reproduction, immunity, growth and development. Ubiquitination and proteasomal degradation of a RLCK VII member, BOTRYTIS-INDUCED KINASE1 (BIK1) play important roles in regulating immune signaling. It remains largely unknown whether most other RLCK VII members undergo ubiquitination and proteasomal degradation. Here, we select the 6-member RLCK VII-4 to examine the potential proteasomal degradation of its members. We find that three closely related RLCK VII-4 members, PBL38 (AvrPphB SUSCEPTIBLE1-LIKE38), PCRK1 (PTI-COMPROMISED RECEPTOR-LIKE CYTOPLASMIC KINASE1), and PCRK2 are under proteasomal control, while the other members in this group are not. Moreover, we demonstrate that PCRK2 undergoes ubiquitination and proteasomal in a kinase activity-dependent manner. However, the plasma membrane (PM) localization of PCRK2 is not required for its degradation. Our work suggests that many other RLCK VII members may undergo ubiquitination and proteasomal degradation to modulate their homeostasis and cellular functions.
•Three closely related RLCK VII-4 members (PBL38, PCRK1, and PCRK2) are under proteasomal control.•PCRK2 is subject to ubiquitination.•The kinase activity of PCRK2 is required for its ubiquitination and proteasomal degradation. |
doi_str_mv | 10.1016/j.bbrc.2021.11.094 |
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•Three closely related RLCK VII-4 members (PBL38, PCRK1, and PCRK2) are under proteasomal control.•PCRK2 is subject to ubiquitination.•The kinase activity of PCRK2 is required for its ubiquitination and proteasomal degradation.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2021.11.094</identifier><identifier>PMID: 34871998</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Degradation ; Gene Expression Regulation, Plant ; Isoenzymes - genetics ; Isoenzymes - metabolism ; PCRK2 ; Phosphorylation ; Plant Leaves - enzymology ; Plant Leaves - genetics ; Proteasome Endopeptidase Complex - metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Proteolysis ; Protoplasts - chemistry ; RLCK ; Sequence Alignment ; Sequence Homology, Amino Acid ; Signal Transduction ; Ubiquitination</subject><ispartof>Biochemical and biophysical research communications, 2022-01, Vol.587, p.113-118</ispartof><rights>2021 Elsevier Inc.</rights><rights>Copyright © 2021 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-fd92225bb0774f28760d28cc9c777f0fa18e680fcb3473b480cc4425913a90143</citedby><cites>FETCH-LOGICAL-c356t-fd92225bb0774f28760d28cc9c777f0fa18e680fcb3473b480cc4425913a90143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2021.11.094$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34871998$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bai, Jiaojiao</creatorcontrib><creatorcontrib>Huang, Guozhong</creatorcontrib><creatorcontrib>Chen, Kexin</creatorcontrib><creatorcontrib>Wang, Ranran</creatorcontrib><creatorcontrib>Lu, Dongping</creatorcontrib><title>A receptor-like cytoplasmic kinase PCRK2 undergoes ubiquitination and proteasomal degradation</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Receptor-like cytoplasmic kinase (RLCK) subfamily VII members are involved in diverse biological processes, like reproduction, immunity, growth and development. Ubiquitination and proteasomal degradation of a RLCK VII member, BOTRYTIS-INDUCED KINASE1 (BIK1) play important roles in regulating immune signaling. It remains largely unknown whether most other RLCK VII members undergo ubiquitination and proteasomal degradation. Here, we select the 6-member RLCK VII-4 to examine the potential proteasomal degradation of its members. We find that three closely related RLCK VII-4 members, PBL38 (AvrPphB SUSCEPTIBLE1-LIKE38), PCRK1 (PTI-COMPROMISED RECEPTOR-LIKE CYTOPLASMIC KINASE1), and PCRK2 are under proteasomal control, while the other members in this group are not. Moreover, we demonstrate that PCRK2 undergoes ubiquitination and proteasomal in a kinase activity-dependent manner. However, the plasma membrane (PM) localization of PCRK2 is not required for its degradation. Our work suggests that many other RLCK VII members may undergo ubiquitination and proteasomal degradation to modulate their homeostasis and cellular functions.
•Three closely related RLCK VII-4 members (PBL38, PCRK1, and PCRK2) are under proteasomal control.•PCRK2 is subject to ubiquitination.•The kinase activity of PCRK2 is required for its ubiquitination and proteasomal degradation.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Degradation</subject><subject>Gene Expression Regulation, Plant</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>PCRK2</subject><subject>Phosphorylation</subject><subject>Plant Leaves - enzymology</subject><subject>Plant Leaves - genetics</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Protein Binding</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteolysis</subject><subject>Protoplasts - chemistry</subject><subject>RLCK</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction</subject><subject>Ubiquitination</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFu1DAQhi0EotvCC3BAPnJJmHEcO5a4VKsCFZWoqiJxQZbjTCpvk3hrJ0h9-2bZwpHTHOb7f818jL1DKBFQfdyVbZt8KUBgiViCkS_YBsFAIRDkS7YBAFUIgz9P2GnOOwBEqcxrdlLJRqMxzYb9OueJPO3nmIoh3BP3j3PcDy6PwfP7MLlM_Hp7803wZeoo3UXKfGnDwxLmdTmHOHE3dXyf4kwux9ENvKO75Lo_uzfsVe-GTG-f5xn78fnidvu1uPr-5XJ7flX4qlZz0XdGCFG3LWgte9FoBZ1ovDdea91D77Ah1UDv20rqqpUNeC-lqA1WzgDK6ox9OPaudzwslGc7huxpGNxEcclWKNC1rpVSKyqOqE8x50S93acwuvRoEexBq93Zg1Z70GoR7ap1Db1_7l_akbp_kb8eV-DTEaD1y9-Bks0-0OSpC6ve2XYx_K__CYOqiUM</recordid><startdate>20220108</startdate><enddate>20220108</enddate><creator>Bai, Jiaojiao</creator><creator>Huang, Guozhong</creator><creator>Chen, Kexin</creator><creator>Wang, Ranran</creator><creator>Lu, Dongping</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20220108</creationdate><title>A receptor-like cytoplasmic kinase PCRK2 undergoes ubiquitination and proteasomal degradation</title><author>Bai, Jiaojiao ; Huang, Guozhong ; Chen, Kexin ; Wang, Ranran ; Lu, Dongping</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-fd92225bb0774f28760d28cc9c777f0fa18e680fcb3473b480cc4425913a90143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Arabidopsis</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Degradation</topic><topic>Gene Expression Regulation, Plant</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>PCRK2</topic><topic>Phosphorylation</topic><topic>Plant Leaves - enzymology</topic><topic>Plant Leaves - genetics</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Protein Binding</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteolysis</topic><topic>Protoplasts - chemistry</topic><topic>RLCK</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bai, Jiaojiao</creatorcontrib><creatorcontrib>Huang, Guozhong</creatorcontrib><creatorcontrib>Chen, Kexin</creatorcontrib><creatorcontrib>Wang, Ranran</creatorcontrib><creatorcontrib>Lu, Dongping</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bai, Jiaojiao</au><au>Huang, Guozhong</au><au>Chen, Kexin</au><au>Wang, Ranran</au><au>Lu, Dongping</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A receptor-like cytoplasmic kinase PCRK2 undergoes ubiquitination and proteasomal degradation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2022-01-08</date><risdate>2022</risdate><volume>587</volume><spage>113</spage><epage>118</epage><pages>113-118</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Receptor-like cytoplasmic kinase (RLCK) subfamily VII members are involved in diverse biological processes, like reproduction, immunity, growth and development. Ubiquitination and proteasomal degradation of a RLCK VII member, BOTRYTIS-INDUCED KINASE1 (BIK1) play important roles in regulating immune signaling. It remains largely unknown whether most other RLCK VII members undergo ubiquitination and proteasomal degradation. Here, we select the 6-member RLCK VII-4 to examine the potential proteasomal degradation of its members. We find that three closely related RLCK VII-4 members, PBL38 (AvrPphB SUSCEPTIBLE1-LIKE38), PCRK1 (PTI-COMPROMISED RECEPTOR-LIKE CYTOPLASMIC KINASE1), and PCRK2 are under proteasomal control, while the other members in this group are not. Moreover, we demonstrate that PCRK2 undergoes ubiquitination and proteasomal in a kinase activity-dependent manner. However, the plasma membrane (PM) localization of PCRK2 is not required for its degradation. Our work suggests that many other RLCK VII members may undergo ubiquitination and proteasomal degradation to modulate their homeostasis and cellular functions.
•Three closely related RLCK VII-4 members (PBL38, PCRK1, and PCRK2) are under proteasomal control.•PCRK2 is subject to ubiquitination.•The kinase activity of PCRK2 is required for its ubiquitination and proteasomal degradation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>34871998</pmid><doi>10.1016/j.bbrc.2021.11.094</doi><tpages>6</tpages></addata></record> |
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subjects | Adenosine Triphosphate - metabolism Amino Acid Sequence Arabidopsis Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Degradation Gene Expression Regulation, Plant Isoenzymes - genetics Isoenzymes - metabolism PCRK2 Phosphorylation Plant Leaves - enzymology Plant Leaves - genetics Proteasome Endopeptidase Complex - metabolism Protein Binding Protein Processing, Post-Translational Proteolysis Protoplasts - chemistry RLCK Sequence Alignment Sequence Homology, Amino Acid Signal Transduction Ubiquitination |
title | A receptor-like cytoplasmic kinase PCRK2 undergoes ubiquitination and proteasomal degradation |
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