Stress granule: Difference between revisions

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== Protein composition of stress granules ==
== Protein composition of stress granules ==


The complete proteome of stress granules is still unknown, but efforts have been made to catalog all of the proteins that have been experimentally demonstrated to transit into stress granules<ref>{{Cite web|url=https://purl.stanford.edu/zv433qj2812|title=Profilin 1, stress granules, and ALS pathogenesis|website=purl.stanford.edu|language=en|access-date=2017-07-26}}</ref><ref>{{Cite journal|last=Aulas|first=Anaïs|last2=Vande Velde|first2=Christine|date=2015|title=Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?|url=https://www.ncbi.nlm.nih.gov/pubmed/26557057|journal=Frontiers in Cellular Neuroscience|volume=9|pages=423|doi=10.3389/fncel.2015.00423|issn=1662-5102|pmc=PMC4615823|pmid=26557057}}</ref>. In 2016, stress granule "cores" were biochemically purified for the first time and proteins were identified in an unbiased manner using mass spectroscopy, leading to the identification of hundreds of new stress granule-localized proteins.<ref>{{Cite journal|last=Jain|first=Saumya|last2=Wheeler|first2=Joshua R.|last3=Walters|first3=Robert W.|last4=Agrawal|first4=Anurag|last5=Barsic|first5=Anthony|last6=Parker|first6=Roy|date=2016-01-28|title=ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure|url=https://www.ncbi.nlm.nih.gov/pubmed/26777405|journal=Cell|volume=164|issue=3|pages=487–498|doi=10.1016/j.cell.2015.12.038|issn=1097-4172|pmc=PMC4733397|pmid=26777405}}</ref>
The complete proteome of stress granules is still unknown, but efforts have been made to catalog all of the proteins that have been experimentally demonstrated to transit into stress granules<ref name=":0">{{Cite web|url=https://purl.stanford.edu/zv433qj2812|title=Profilin 1, stress granules, and ALS pathogenesis|website=purl.stanford.edu|language=en|access-date=2017-07-26}}</ref><ref name=":1">{{Cite journal|last=Aulas|first=Anaïs|last2=Vande Velde|first2=Christine|date=2015|title=Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?|url=https://www.ncbi.nlm.nih.gov/pubmed/26557057|journal=Frontiers in Cellular Neuroscience|volume=9|pages=423|doi=10.3389/fncel.2015.00423|issn=1662-5102|pmc=PMC4615823|pmid=26557057}}</ref>. In 2016, stress granule "cores" were biochemically purified for the first time and proteins were identified in an unbiased manner using mass spectroscopy, leading to the identification of hundreds of new stress granule-localized proteins.<ref name=":2">{{Cite journal|last=Jain|first=Saumya|last2=Wheeler|first2=Joshua R.|last3=Walters|first3=Robert W.|last4=Agrawal|first4=Anurag|last5=Barsic|first5=Anthony|last6=Parker|first6=Roy|date=2016-01-28|title=ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure|url=https://www.ncbi.nlm.nih.gov/pubmed/26777405|journal=Cell|volume=164|issue=3|pages=487–498|doi=10.1016/j.cell.2015.12.038|issn=1097-4172|pmc=PMC4733397|pmid=26777405}}</ref>


The following is a list of proteins that have been demonstrated to localize to stress granules:
The following is a list of proteins that have been demonstrated to localize to stress granules (compiled from <ref name=":0" /><ref name=":1" /><ref name=":2" />):


{| class="“wikitable”"
{| class="wikitable “wikitable”"
|-
|-
! Gene ID
! Gene ID
Line 34: Line 34:
| ACTBL2
| ACTBL2
| Beta-actin-like protein 2
| Beta-actin-like protein 2
| <ref name=":2" />
⚫
| <ref>{{Cite journal|last=Jain|first=Saumya|last2=Wheeler|first2=Joshua R.|last3=Walters|first3=Robert W.|last4=Agrawal|first4=Anurag|last5=Barsic|first5=Anthony|last6=Parker|first6=Roy|date=2016-01-28|title=ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure|url=https://www.ncbi.nlm.nih.gov/pubmed/26777405|journal=Cell|volume=164|issue=3|pages=487–498|doi=10.1016/j.cell.2015.12.038|issn=1097-4172|pmc=PMC4733397|pmid=26777405}}</ref>
|-
|-
| ACTR1A
| ACTR1A
| ACTR1A
| ACTR1A
| Alpha-centractin
| Alpha-centractin
|<ref name=":2" />
|
|-
|ACTR1B
|ACTR1B
|Beta-centractin
|<ref name=":2" />
|-
|ADAR
|ADAR1
|Adenosine Deaminase, RNA Specific
|<ref>{{Cite journal|last=Weissbach|first=Rebekka|last2=Scadden|first2=A. D. J.|date=March 2012|title=Tudor-SN and ADAR1 are components of cytoplasmic stress granules|url=https://www.ncbi.nlm.nih.gov/pubmed/22240577|journal=RNA (New York, N.Y.)|volume=18|issue=3|pages=462–471|doi=10.1261/rna.027656.111|issn=1469-9001|pmc=PMC3285934|pmid=22240577}}</ref><ref name=":2" />
|-
|AGO1
|Argonaute 1
|Argonaute 1, RISC Catalytic Component
⚫
|<ref>{{Cite journal|last=Gallois-Montbrun|first=Sarah|last2=Kramer|first2=Beatrice|last3=Swanson|first3=Chad M.|last4=Byers|first4=Helen|last5=Lynham|first5=Steven|last6=Ward|first6=Malcolm|last7=Malim|first7=Michael H.|date=March 2007|title=Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules|url=https://www.ncbi.nlm.nih.gov/pubmed/17166910|journal=Journal of Virology|volume=81|issue=5|pages=2165–2178|doi=10.1128/JVI.02287-06|issn=0022-538X|pmc=PMC1865933|pmid=17166910}}</ref>
|}
|}


Revision as of 20:55, 26 July 2017

Stress granules are dense aggregations in the cytosol composed of proteins & RNAs that appear when the cell is under stress.[1] The RNA molecules stored are stalled translation pre-initiation complexes: failed attempts to make protein from mRNA. Stress granules are 100–200 nm in size, not surrounded by membrane, and associated with the endoplasmatic reticulum.[2] Note that there are also nuclear stress granules. This article is about the cytosolic variety.

Proposed functions

Stress granules may function to protect RNAs from harmful conditions, thus their appearance under stress.[3] The accumulation of RNAs into dense globules could keep them from reacting with harmful chemicals and safe-guard the information coded in their RNA sequence.

Stress granules might also function as a decision point for untranslated mRNAs. Molecules can go down one of three paths: further storage, degradation, or re-initiation of translation.[4]

The stress proteins that are the main component of stress granules in plant cells are molecular chaperones that sequester, protect, and possibly repair proteins that unfold during heat and other types of stress.[5][6] Therefore, any association of mRNAs with stress granules may simply be a side effect of the association of partially unfolded RNA-binding proteins with stress granules,[7] similar to the association of mRNAs with proteasomes.[8]

Formation

Environmental stress triggers a series of signals which eventually lead to formation of stress granules. Early on, it involves phosphorylation of eukaryotic translation initiation factor eIF2α. Further downstream, prion-like aggregation of the protein TIA-1 leads to the formation of stress granules. The term prion-like is used because aggregation of TIA-1 is concentration dependent, inhibited by chaperones, and because the aggregates are resistant to proteases.[9] It has also been proposed that microtubules play a role in the formation of stress granules, maybe by transporting granule components. This hypothesis is based on the fact that disruption of microtubules with the chemical nocodazole blocks the appearance of the granules.[10] Furthermore, many signaling molecules were shown to regulate the formation or dynamics of stress granules; these include the master energy sensor AMP-activated protein kinase (AMPK),[11] the O-GlcNAc transferase enzyme (OGT)[12], and the pro-apoptotic kinase ROCK1.[13]

Connection with processing bodies

Stress granules and processing bodies share RNA and protein components, both appear under stress, and can physically associate with one another. While stress granules are associated with mRNAs, processing bodies are thought to be places of mRNA degradation. It has been proposed that mRNAs selected for degradation are passed from stress granules to processing bodies.[14]

Protein composition of stress granules

The complete proteome of stress granules is still unknown, but efforts have been made to catalog all of the proteins that have been experimentally demonstrated to transit into stress granules[15][16]. In 2016, stress granule "cores" were biochemically purified for the first time and proteins were identified in an unbiased manner using mass spectroscopy, leading to the identification of hundreds of new stress granule-localized proteins.[17]

The following is a list of proteins that have been demonstrated to localize to stress granules (compiled from [15][16][17]):

Gene ID Protein Name Description References
ACTBL2 ACTBL2 Beta-actin-like protein 2 [17]
ACTR1A ACTR1A Alpha-centractin [17]
ACTR1B ACTR1B Beta-centractin [17]
ADAR ADAR1 Adenosine Deaminase, RNA Specific [18][17]
AGO1 Argonaute 1 Argonaute 1, RISC Catalytic Component [19]

References

  1. ^ Gutierrez-Beltran E, Moschou PN, Smertenko AP, Bozhkov PV (March 2015). "Tudor Staphylococcal Nuclease Links Formation of Stress Granules and Processing Bodies with mRNA Catabolism in Arabidopsis". Plant Cell. 27: 926–43. doi:10.1105/tpc.114.134494. PMC 4558657. PMID 25736060.
  2. ^ Kayali F, Montie HL, Rafols JA, DeGracia DJ (2005). "Prolonged translation arrest in reperfused hippocampal cornu Ammonis 1 is mediated by stress granules". Neuroscience. 134 (4): 1223–45. doi:10.1016/j.neuroscience.2005.05.047. PMID 16055272.
  3. ^ Nover L, Scharf KD, Neumann D (Mar 1989). "Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs". Mol Cell Biol. 9 (3): 1298–308. PMC 362722. PMID 2725500.
  4. ^ Paul J. Anderson, Brigham and Women's Hospital
  5. ^ Forreiter C, Kirschner M, Nover L (Dec 1997). "Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo". Plant Cell. 9 (12): 2171–81. doi:10.1105/tpc.9.12.2171. PMC 157066. PMID 9437862.
  6. ^ Löw D, Brändle K, Nover L, Forreiter C (Sep 2000). "Cytosolic heat-stress proteins Hsp17.7 class I and Hsp17.3 class II of tomato act as molecular chaperones in vivo". Planta. 211 (4): 575–82. doi:10.1007/s004250000315. PMID 11030557.
  7. ^ Stuger R, Ranostaj S, Materna T, Forreiter C (May 1999). "Messenger RNA-binding properties of nonpolysomal ribonucleoproteins from heat-stressed tomato cells". Plant Physiol. 120 (1): 23–32. doi:10.1104/pp.120.1.23. PMC 59255. PMID 10318680.
  8. ^ Schmid HP, Akhayat O, Martins De Sa C, Puvion F, Koehler K, Scherrer K (Jan 1984). "The prosome: an ubiquitous morphologically distinct RNP particle associated with repressed mRNPs and containing specific ScRNA and a characteristic set of proteins". EMBO J. 3 (1): 29–34. PMC 557293. PMID 6200323.
  9. ^ Gilks N, Kedersha N, Ayodele M, et al. (Dec 2004). "Stress granule assembly is mediated by prion-like aggregation of TIA-1". Mol Biol Cell. 15 (12): 5383–98. doi:10.1091/mbc.E04-08-0715. PMC 532018. PMID 15371533.
  10. ^ Ivanov PA, Chudinova EM, Nadezhdina ES (Nov 2003). "Disruption of microtubules inhibits cytoplasmic ribonucleoprotein stress granule formation". Exp. Cell Res. 290 (2): 227–33. doi:10.1016/S0014-4827(03)00290-8. PMID 14567982.
  11. ^ Mahboubi, Hicham; Barisé, Ramla; Stochaj, Ursula (2015-07-01). "5′-AMP-activated protein kinase alpha regulates stress granule biogenesis". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853 (7): 1725–1737. doi:10.1016/j.bbamcr.2015.03.015.
  12. ^ Ohn, Takbum; Kedersha, Nancy; Hickman, Tyler; Tisdale, Sarah; Anderson, Paul (2008). "A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly". Nature Cell Biology. 10 (10): 1224–1231. doi:10.1038/ncb1783. PMC 4318256. PMID 18794846.
  13. ^ Tsai, Nien-Pei; Wei, Li-Na (2010-04-01). "RhoA/ROCK1 signaling regulates stress granule formation and apoptosis". Cellular Signalling. 22 (4): 668–675. doi:10.1016/j.cellsig.2009.12.001. PMC 2815184. PMID 20004716.
  14. ^ Kedersha N, Stoecklin G, Ayodele M, et al. (Jun 2005). "Stress granules and processing bodies are dynamically linked sites of mRNP remodeling". J. Cell Biol. 169 (6): 871–84. doi:10.1083/jcb.200502088. PMC 2171635. PMID 15967811.
  15. ^ a b "Profilin 1, stress granules, and ALS pathogenesis". purl.stanford.edu. Retrieved 2017-07-26.
  16. ^ a b Aulas, Anaïs; Vande Velde, Christine (2015). "Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?". Frontiers in Cellular Neuroscience. 9: 423. doi:10.3389/fncel.2015.00423. ISSN 1662-5102. PMC 4615823. PMID 26557057.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  17. ^ a b c d e f Jain, Saumya; Wheeler, Joshua R.; Walters, Robert W.; Agrawal, Anurag; Barsic, Anthony; Parker, Roy (2016-01-28). "ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure". Cell. 164 (3): 487–498. doi:10.1016/j.cell.2015.12.038. ISSN 1097-4172. PMC 4733397. PMID 26777405.{{cite journal}}: CS1 maint: PMC format (link)
  18. ^ Weissbach, Rebekka; Scadden, A. D. J. (March 2012). "Tudor-SN and ADAR1 are components of cytoplasmic stress granules". RNA (New York, N.Y.). 18 (3): 462–471. doi:10.1261/rna.027656.111. ISSN 1469-9001. PMC 3285934. PMID 22240577.{{cite journal}}: CS1 maint: PMC format (link)
  19. ^ Gallois-Montbrun, Sarah; Kramer, Beatrice; Swanson, Chad M.; Byers, Helen; Lynham, Steven; Ward, Malcolm; Malim, Michael H. (March 2007). "Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules". Journal of Virology. 81 (5): 2165–2178. doi:10.1128/JVI.02287-06. ISSN 0022-538X. PMC 1865933. PMID 17166910.{{cite journal}}: CS1 maint: PMC format (link)

External links

Review articles:

Laboratories:

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