BRI1-associated receptor kinase 1: Difference between revisions

Add links
From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
Scotanist (talk | contribs)
96 edits
Added section on molecular basis for diverse functions
Scotanist (talk | contribs)
96 edits
→‎Roles in plant development: Added new subsection. Re-formatted role in defense
Line 35: Line 35:


=== Brassinosteroid signalling ===
=== Brassinosteroid signalling ===
[[File:BRI1-BAK1 diagram.jpg|thumb|300x300px|Diagram of BAK1 in complex with BRI1 for brassinosteroid signalling]]
[[File:BRI1-BAK1 diagram.jpg|thumb|300x300px|Diagram of BAK1 in complex with BRI1 during brassinosteroid signalling]]
BAK1 was initially identified for its role in [[brassinosteroid]] signalling.<ref>{{cite journal | vauthors = Li J, Wen J, Lease KA, Doke JT, Tax FE, Walker JC | title = BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling | journal = Cell | volume = 110 | issue = 2 | pages = 213–22 | date = July 2002 | pmid = 12150929 }}</ref> Brassinosteroid is a major [[plant hormone]] that has many roles and is often associated with [[Plant cell|cell]] elongation.<ref name="Belkhadir_2015" /> BAK1 binds to the brassinosteroid receptor [[Brassinosteroid Insensitive-1|BRASSINOSTEROID INSENSITIVE 1]] (BRI1).
BAK1 was initially identified for its role in [[brassinosteroid]] signalling.<ref name=":1">{{cite journal | vauthors = Li J, Wen J, Lease KA, Doke JT, Tax FE, Walker JC | title = BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling | journal = Cell | volume = 110 | issue = 2 | pages = 213–22 | date = July 2002 | pmid = 12150929 }}</ref> Brassinosteroid is a major [[plant hormone]] that has many roles and is often associated with [[Plant cell|cell]] elongation.<ref name="Belkhadir_2015" /> BAK1 binds to the brassinosteroid receptor [[Brassinosteroid Insensitive-1|BRASSINOSTEROID INSENSITIVE 1]] (BRI1) and this then triggers a [[phosphorylation cascade]] that leads to a change in [[Gene expression|expression]] of multiple genes.<ref name=":1" />


=== Defense signalling ===
=== Defense signalling ===


BAK1 is involved in signalling by [[FLS2]] and EFR. Plants carrying mutations in BAK1 show normal [[flagellin]] binding but abnormal early and late flagellin-triggered responses, indicating that BAK1 acts as a positive regulator in signalling. The bak1-mutant plants also show a reduction in early, but not late, EF-Tu-triggered responses. The decrease in responses to PAMPs is not due to reduced sensitivity to brassinosteroids. In vivo FLS2 and BAK1 form a complex, in a specific ligand-dependent manner, within the first minutes of stimulation with flagellin. Thus, BAK1 is not only associated with developmental regulation through the plant hormone receptor BRI1, but also has a functional role in PRR-dependent signalling, which initiates innate immunity.<ref name="pmid17625569">{{cite journal | vauthors = Chinchilla D, Zipfel C, Robatzek S, Kemmerling B, Nürnberger T, Jones JD, Felix G, Boller T | title = A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence | journal = Nature | volume = 448 | issue = 7152 | pages = 497–500 | date = July 2007 | pmid = 17625569 | doi = 10.1038/nature05999 }}</ref>
BAK1 is also critical for [[Plant disease resistance|plant immunity]] and plants the lack BAK1 show a much greater susceptibility to bacterial infections. <ref name="pmid17625569">{{cite journal|vauthors=Chinchilla D, Zipfel C, Robatzek S, Kemmerling B, Nürnberger T, Jones JD, Felix G, Boller T|date=July 2007|title=A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence|journal=Nature|volume=448|issue=7152|pages=497–500|doi=10.1038/nature05999|pmid=17625569}}</ref> Plants are able to perceive [[bacteria]] by recognizing specific molecular signatures or '[[Bacterial effector protein|effectors]]'. One of these signatures is bacterial-derived [[flagellin]]. Plants perceive flagellin when it binds to the receptor [[FLS2]]. When flagellin is perceived by FLS2, this strongly promotes the interaction between FLS2 and BAK1 and this then leads to changes in gene expression that promote defense against bacteria. <ref name="pmid17625569" />


In addition to flagellin, plants are also able to perceive other bacterial effectors. One of these, [[EF-Tu]] is perceived by the [[EF-Tu receptor]] (EFR). Similar to FLS2, BAK1 is required for EFR function. <ref name=":2">{{Cite journal|last=Jordá|first=Lucía|last2=Sopeña-Torres|first2=Sara|last3=Escudero|first3=Viviana|last4=Nuñez-Corcuera|first4=Beatriz|last5=Delgado-Cerezo|first5=Magdalena|last6=Torii|first6=Keiko U.|last7=Molina|first7=Antonio|date=2016|title=ERECTA and BAK1 Receptor Like Kinases Interact to Regulate Immune Responses in Arabidopsis|url=https://www.frontiersin.org/articles/10.3389/fpls.2016.00897/full#B54|journal=Frontiers in Plant Science|language=English|volume=7|doi=10.3389/fpls.2016.00897|issn=1664-462X}}</ref>
⚫
== Molecular basis for diverse functional roles ==

The LRR-RK ERECTA (ER) may also promote plant defense, in concert with BAK1. <ref name=":2" />

=== Regulation of stomatal development ===
Along with its role in plant defense, the ER:BAK1 complex also repress the development of [[Stoma|stomata]] in leaves. Mutations in BAK1 and ER lead in increase in the number of stomata. <ref name=":2" />

⚫
=== Molecular basis for diverse functional roles ===
The diverse functional roles of BAK1 are brought about through its binding to a large number of receptors. <ref name=":0" /> Interestingly however, many of the molecular components downstream of these receptor:BAK1 complexes are shared between these signalling pathways (for example, BR SIGNALLING KINASE 1 (BSK1) is a positive regulator of both BRI1:BAK1 signalling <ref>{{Cite journal|last=Tang|first=Wenqiang|last2=Kim|first2=Tae-Wuk|last3=Oses-Prieto|first3=Juan A.|last4=Sun|first4=Yu|last5=Deng|first5=Zhiping|last6=Zhu|first6=Shengwei|last7=Wang|first7=Ruiju|last8=Burlingame|first8=Alma L.|last9=Wang|first9=Zhi-Yong|date=2008-07-25|title=BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis|url=http://science.sciencemag.org/content/321/5888/557|journal=Science|language=en|volume=321|issue=5888|pages=557–560|doi=10.1126/science.1156973|issn=0036-8075|pmid=18653891}}</ref> and FLS2:BAK1 signalling<ref>{{Cite journal|last=Shi|first=Hua|last2=Shen|first2=Qiujing|last3=Qi|first3=Yiping|last4=Yan|first4=Haojie|last5=Nie|first5=Haozhen|last6=Chen|first6=Yongfang|last7=Zhao|first7=Ting|last8=Katagiri|first8=Fumiaki|last9=Tang|first9=Dingzhong|date=2013-03-01|title=BR-SIGNALING KINASE1 Physically Associates with FLAGELLIN SENSING2 and Regulates Plant Innate Immunity in Arabidopsis|url=http://www.plantcell.org/content/25/3/1143|journal=The Plant Cell|language=en|volume=25|issue=3|pages=1143–1157|doi=10.1105/tpc.112.107904|issn=1040-4651|pmid=23532072}}</ref>). It is currently unclear how cells are able to distinguish between a BSK1 which has been activated by BRI1 or FLS2. One recent study has shown that BRI1 and FLS2 localize to different 'nano-domains' on the cell membrane and so it is possible that this spacial-separation accounts for the very different signal outputs. <ref>{{Cite journal|last=Bücherl|first=Christoph A|last2=Jarsch|first2=Iris K|last3=Schudoma|first3=Christian|last4=Segonzac|first4=Cécile|last5=Mbengue|first5=Malick|last6=Robatzek|first6=Silke|last7=MacLean|first7=Daniel|last8=Ott|first8=Thomas|last9=Zipfel|first9=Cyril|date=2017-03-06|title=Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains|url=https://elifesciences.org/articles/25114|journal=eLife|language=en|volume=6|doi=10.7554/eLife.25114|issn=2050-084X}}</ref>
The diverse functional roles of BAK1 are brought about through its binding to a large number of receptors. <ref name=":0" /> Interestingly however, many of the molecular components downstream of these receptor:BAK1 complexes are shared between these signalling pathways (for example, BR SIGNALLING KINASE 1 (BSK1) is a positive regulator of both BRI1:BAK1 signalling <ref>{{Cite journal|last=Tang|first=Wenqiang|last2=Kim|first2=Tae-Wuk|last3=Oses-Prieto|first3=Juan A.|last4=Sun|first4=Yu|last5=Deng|first5=Zhiping|last6=Zhu|first6=Shengwei|last7=Wang|first7=Ruiju|last8=Burlingame|first8=Alma L.|last9=Wang|first9=Zhi-Yong|date=2008-07-25|title=BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis|url=http://science.sciencemag.org/content/321/5888/557|journal=Science|language=en|volume=321|issue=5888|pages=557–560|doi=10.1126/science.1156973|issn=0036-8075|pmid=18653891}}</ref> and FLS2:BAK1 signalling<ref>{{Cite journal|last=Shi|first=Hua|last2=Shen|first2=Qiujing|last3=Qi|first3=Yiping|last4=Yan|first4=Haojie|last5=Nie|first5=Haozhen|last6=Chen|first6=Yongfang|last7=Zhao|first7=Ting|last8=Katagiri|first8=Fumiaki|last9=Tang|first9=Dingzhong|date=2013-03-01|title=BR-SIGNALING KINASE1 Physically Associates with FLAGELLIN SENSING2 and Regulates Plant Innate Immunity in Arabidopsis|url=http://www.plantcell.org/content/25/3/1143|journal=The Plant Cell|language=en|volume=25|issue=3|pages=1143–1157|doi=10.1105/tpc.112.107904|issn=1040-4651|pmid=23532072}}</ref>). It is currently unclear how cells are able to distinguish between a BSK1 which has been activated by BRI1 or FLS2. One recent study has shown that BRI1 and FLS2 localize to different 'nano-domains' on the cell membrane and so it is possible that this spacial-separation accounts for the very different signal outputs. <ref>{{Cite journal|last=Bücherl|first=Christoph A|last2=Jarsch|first2=Iris K|last3=Schudoma|first3=Christian|last4=Segonzac|first4=Cécile|last5=Mbengue|first5=Malick|last6=Robatzek|first6=Silke|last7=MacLean|first7=Daniel|last8=Ott|first8=Thomas|last9=Zipfel|first9=Cyril|date=2017-03-06|title=Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains|url=https://elifesciences.org/articles/25114|journal=eLife|language=en|volume=6|doi=10.7554/eLife.25114|issn=2050-084X}}</ref>


Revision as of 08:55, 10 May 2018

Brassinosteroid insensitive 1-associated receptor kinase 1
Identifiers
OrganismA. thaliana (thale cress)
SymbolBAK1
Entrez829480
RefSeq (mRNA)NM_119497.4
RefSeq (Prot)NP_567920.1
UniProtQ94F62
Other data
EC number2.7.1.37
Chromosome4: 16.09 - 16.09 Mb
Search for
StructuresSwiss-model
DomainsInterPro

BRI1-associated receptor kinase 1 (BAK1- also known as somatic embryogenesis receptor kinase 3 or SERK3) is an important plant protein that has diverse functions in plant development.

Structure

BAK1 belongs to a large group of plant proteins known as the Leucine-rich repeat receptor kinases (LRR-RKs). In the model plant species Arabidopsis thaliana, BAK1 and 4 other closely related proteins form a sub-group within the LRR-RK family, known as the somatic embryogenesis receptor kinases (SERKs). All 5 SERKs are transmembrane proteins. They consist of an extracellular domain, a single transmembrane pass and an intracellular domain. The extracellular domain is composed of several leucine rich repeats, and the intracellular domain functions as a protein kinase.[1] BAK1 is thought to interact with many other LRR-RKs and the signalling output of BAK1 is dependent on its binding partner [2]

Roles in plant development

Brassinosteroid signalling

Diagram of BAK1 in complex with BRI1 during brassinosteroid signalling

BAK1 was initially identified for its role in brassinosteroid signalling.[3] Brassinosteroid is a major plant hormone that has many roles and is often associated with cell elongation.[1] BAK1 binds to the brassinosteroid receptor BRASSINOSTEROID INSENSITIVE 1 (BRI1) and this then triggers a phosphorylation cascade that leads to a change in expression of multiple genes.[3]

Defense signalling

BAK1 is also critical for plant immunity and plants the lack BAK1 show a much greater susceptibility to bacterial infections. [4] Plants are able to perceive bacteria by recognizing specific molecular signatures or 'effectors'. One of these signatures is bacterial-derived flagellin. Plants perceive flagellin when it binds to the receptor FLS2. When flagellin is perceived by FLS2, this strongly promotes the interaction between FLS2 and BAK1 and this then leads to changes in gene expression that promote defense against bacteria. [4]

In addition to flagellin, plants are also able to perceive other bacterial effectors. One of these, EF-Tu is perceived by the EF-Tu receptor (EFR). Similar to FLS2, BAK1 is required for EFR function. [5]

The LRR-RK ERECTA (ER) may also promote plant defense, in concert with BAK1. [5]

Regulation of stomatal development

Along with its role in plant defense, the ER:BAK1 complex also repress the development of stomata in leaves. Mutations in BAK1 and ER lead in increase in the number of stomata. [5]

Molecular basis for diverse functional roles

The diverse functional roles of BAK1 are brought about through its binding to a large number of receptors. [2] Interestingly however, many of the molecular components downstream of these receptor:BAK1 complexes are shared between these signalling pathways (for example, BR SIGNALLING KINASE 1 (BSK1) is a positive regulator of both BRI1:BAK1 signalling [6] and FLS2:BAK1 signalling[7]). It is currently unclear how cells are able to distinguish between a BSK1 which has been activated by BRI1 or FLS2. One recent study has shown that BRI1 and FLS2 localize to different 'nano-domains' on the cell membrane and so it is possible that this spacial-separation accounts for the very different signal outputs. [8]

References

  1. ^ a b Belkhadir Y, Jaillais Y (April 2015). "The molecular circuitry of brassinosteroid signaling". The New Phytologist. 206 (2): 522–40. doi:10.1111/nph.13269. PMID 25615890.
  2. ^ a b Smakowska-Luzan E, Mott GA, Parys K, Stegmann M, Howton TC, Layeghifard M, Neuhold J, Lehner A, Kong J, Grünwald K, Weinberger N, Satbhai SB, Mayer D, Busch W, Madalinski M, Stolt-Bergner P, Provart NJ, Mukhtar MS, Zipfel C, Desveaux D, Guttman DS, Belkhadir Y (January 2018). "An extracellular network of Arabidopsis leucine-rich repeat receptor kinases". Nature. 553 (7688): 342–346. doi:10.1038/nature25184. PMID 29320478.
  3. ^ a b Li J, Wen J, Lease KA, Doke JT, Tax FE, Walker JC (July 2002). "BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling". Cell. 110 (2): 213–22. PMID 12150929.
  4. ^ a b Chinchilla D, Zipfel C, Robatzek S, Kemmerling B, Nürnberger T, Jones JD, Felix G, Boller T (July 2007). "A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence". Nature. 448 (7152): 497–500. doi:10.1038/nature05999. PMID 17625569.
  5. ^ a b c Jordá, Lucía; Sopeña-Torres, Sara; Escudero, Viviana; Nuñez-Corcuera, Beatriz; Delgado-Cerezo, Magdalena; Torii, Keiko U.; Molina, Antonio (2016). "ERECTA and BAK1 Receptor Like Kinases Interact to Regulate Immune Responses in Arabidopsis". Frontiers in Plant Science. 7. doi:10.3389/fpls.2016.00897. ISSN 1664-462X.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  6. ^ Tang, Wenqiang; Kim, Tae-Wuk; Oses-Prieto, Juan A.; Sun, Yu; Deng, Zhiping; Zhu, Shengwei; Wang, Ruiju; Burlingame, Alma L.; Wang, Zhi-Yong (2008-07-25). "BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis". Science. 321 (5888): 557–560. doi:10.1126/science.1156973. ISSN 0036-8075. PMID 18653891.
  7. ^ Shi, Hua; Shen, Qiujing; Qi, Yiping; Yan, Haojie; Nie, Haozhen; Chen, Yongfang; Zhao, Ting; Katagiri, Fumiaki; Tang, Dingzhong (2013-03-01). "BR-SIGNALING KINASE1 Physically Associates with FLAGELLIN SENSING2 and Regulates Plant Innate Immunity in Arabidopsis". The Plant Cell. 25 (3): 1143–1157. doi:10.1105/tpc.112.107904. ISSN 1040-4651. PMID 23532072.
  8. ^ Bücherl, Christoph A; Jarsch, Iris K; Schudoma, Christian; Segonzac, Cécile; Mbengue, Malick; Robatzek, Silke; MacLean, Daniel; Ott, Thomas; Zipfel, Cyril (2017-03-06). "Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains". eLife. 6. doi:10.7554/eLife.25114. ISSN 2050-084X.{{cite journal}}: CS1 maint: unflagged free DOI (link)

External links

Retrieved from "https://en.wikipedia.org/w/index.php?title=BRI1-associated_receptor_kinase_1&oldid=840500561"