Advertisement
Journal Article
SOCS: physiological suppressors of cytokine signaling
D.L. Krebs, D.J. Hilton
Journal of Cell Science 2000 113: 2813-2819;

Summary

Cytokines regulate cellular behavior by interacting with receptors on the plasma membrane of target cells and activating intracellular signal transduction cascades such as the JAK-STAT pathway. Suppressors of cytokine signaling (SOCS) proteins negatively regulate cytokine signaling. The SOCS family consists of eight proteins: SOCS1-SOCS7 and CIS, each of which contains a central Src-homology 2 (SH2) domain and a C-terminal SOCS box. The expression of CIS, SOCS1, SOCS2 and SOCS3 is induced in response to stimulation by a wide variety of cytokines, and overexpression of these proteins in cell lines results in inhibition of cytokine signaling. Thus, SOCS proteins appear to form part of a classical negative feedback loop. The analysis of mice lacking SOCS1 has revealed that it is critical in the negative regulation of IFN(gamma) signaling and in the differentiation of T cells. Additionally, the analysis of mouse embryos lacking SOCS3 suggests that SOCS3 negatively regulates fetal liver erythropoiesis, probably through its ability to modulate erythropoietin (Epo) signaling. Thus, the use of gene targeting has confirmed that SOCS proteins regulate cytokine signaling in a physiological setting.

REFERENCES

    1. Alexander, W. S.,
    2. Starr, R.,
    3. Fenner, J. E.,
    4. Scott, C. L.,
    5. Handman, E.,
    6. Sprigg, N. S.,
    7. Corbin, J. E.,
    8. Cornish, A. L.,
    9. Darwiche, R.,
    10. Owczarek, C. M.,
    11. Kay, T. W.,
    12. Nicola, N. A.,
    13. Hertzog, P. J.,
    14. Metcalf, D. and
    15. Hilton, D. J.
    (1999). SOCS1 is a critical inhibitor of interferon gamma signaling and prevents the potentially fatal neonatal actions of this cytokine. Cell 98, 597–608
    OpenUrlCrossRefPubMedWeb of Science
    1. Auernhammer, C. and
    2. Melmed, S.
    (1999). Interleukin-11 stimulates proopiomelanocortin gene expression and adrenocorticotropin secretion in corticotroph cells: evidence for a redundant cytokine network in the hypothalamo-pituitary-adrenal axis. Endocrinology 140, 1559–1566
    OpenUrlCrossRefPubMedWeb of Science
    1. Bjorbaek, C.,
    2. Elmquist, J. K.,
    3. Frantz, J. D.,
    4. Shoelson, S. E. and
    5. Flier, J. S.
    (1998). Identification of SOCS-3 as a potential mediator of central leptin resistance. Mol. Cell 1, 619–625
    OpenUrlCrossRefPubMedWeb of Science
    1. Bjorbaek, C.,
    2. Elmquist, J. K.,
    3. El-Haschimi, K.,
    4. Kelly, J.,
    5. Ahima, R. S.,
    6. Hileman, S. and
    7. Flier, J. S.
    (1999). Activation of SOCS-3 messenger ribonucleic acid in the hypothalamus by ciliary neurotrophic factor. Endocrinology 140, 2035–2043
    OpenUrlCrossRefPubMedWeb of Science
    1. Bjorbaek, C.,
    2. El-Haschimi, K.,
    3. Frantz, J. D. and
    4. Flier, J. S.
    (1999). The role of SOCS-3 in leptin signaling and leptin resistance. J. Biol. Chem 274, 30059–30065
    OpenUrlAbstract/FREE Full Text
    1. Bousquet, C.,
    2. Susini, C. and
    3. Melmed, S.
    (1999). Inhibitory roles for SHP-1 and SOCS-3 following pituitary proopiomelanocortin induction by leukemia inhibitory factor. J. Clin. Invest 104, 1277–1285
    OpenUrlCrossRefPubMedWeb of Science
    1. Cohney, S. J.,
    2. Sanden, D.,
    3. Cacalano, N. A.,
    4. Yoshimura, A.,
    5. Mui, A.,
    6. Migone, T. S. and
    7. Johnston, J. A.
    (1999). SOCS-3 is tyrosine phosphorylated in response to interleukin-2 and suppresses STAT5 phosphorylation and lymphocyte proliferation. Mol. Cell. Biol 19, 4980–4988
    OpenUrlAbstract/FREE Full Text
    1. Darnell, J. E.
    (1997). STATs and gene regulation. Science 277, 1630–1635
    OpenUrlAbstract/FREE Full Text
    1. Davey, H. W.,
    2. McLachlan, M. J.,
    3. Wilkins, R. J.,
    4. Hilton, D. J. and
    5. Adams, T. E.
    (1999). STAT5b mediates the GH-induced expression of SOCS-2 and SOCS-3 mRNA in the liver. Mol. Cell. Endocrinol 158, 111–116
    OpenUrlCrossRefPubMedWeb of Science
    1. De Sepulveda, P.,
    2. Okkenhaug, K.,
    3. La Rose, J.,
    4. Hawley, R. G.,
    5. Dubreuil, P. and
    6. Rottapel, R.
    (1999). Socs1 binds to multiple signalling proteins and suppresses Steel factor-dependent proliferation. EMBO J 18, 904–915
    OpenUrlAbstract
    1. Dey, B. R.,
    2. Spence, S. L.,
    3. Nissley, P. and
    4. Furlanetto, R. W.
    (1998). Interaction of human suppressor of cytokine signaling (SOCS)-2 with the insulin-like growth factor-1 receptor. J. Biol. Chem 273, 24095–24101
    OpenUrlAbstract/FREE Full Text
    1. Endo, T. A.,
    2. Masuhara, M.,
    3. Yokouchi, M.,
    4. Suzuki, R.,
    5. Sakamoto, H.,
    6. Mitsui, K.,
    7. Matsumoto, A.,
    8. Tanimura, S.,
    9. Ohtsubo, M.,
    10. Misawa, H.,
    11. Miyazaki, T.,
    12. Leonor, N.,
    13. Taniguchi, T.,
    14. Fujita, T.,
    15. Kanakura, Y.,
    16. Komiya, S. and
    17. Yoshimura, A.
    (1997). A new protein containing an SH2 domain that inhibits JAK kinases. Nature 387, 921–924
    OpenUrlCrossRefPubMedWeb of Science
    1. Gobert, S.,
    2. Chretien, S.,
    3. Gouilleux, F.,
    4. Muller, O.,
    5. Pallard, C.,
    6. Dusanter-Fourt, Il,
    7. Groner, B.,
    8. Lacombe, C.,
    9. Gisselbrecht, S. and
    10. Mayeux, P.
    (1996). Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor critical for STAT5 activation. EMBO J 15, 2434–2441
    OpenUrlPubMedWeb of Science
    1. Gresser, L.,
    2. Aguet, M.,
    3. Morel-Maroger, L.,
    4. Woodrow, D.,
    5. Puvion-Dutilleul, F.,
    6. Gullion, J.-C. and
    7. Maury, C.
    (1981). Electrophoretically pure mouseinterferon inhibits growth, induces liver and kidney lesions, and kills suckling mice. Am. J. Pathol 102, 396–402
    OpenUrlPubMedWeb of Science
    1. Hansen, J. A.,
    2. Lindberg, K.,
    3. Hilton, D. J.,
    4. Nielsen, J. H. and
    5. Billestrup, N.
    (1999). Mechanism of inhibition of growth hormone receptor signaling by suppressor of cytokine signaling proteins. Mol. Endocrinol 13, 1832–1843
    OpenUrlCrossRefPubMedWeb of Science
    1. Hershko, A. and
    2. Ciechanover, A.
    (1998). The ubiquitin system. Annu. Rev. Biochem 67, 425–479
    OpenUrlCrossRefPubMedWeb of Science
    1. Hilton, D. J.,
    2. Richardson, R. T.,
    3. Alexander, W. S.,
    4. Viney, E. M.,
    5. Willson, T. A.,
    6. Sprigg, N. S.,
    7. Starr, R.,
    8. Nicholson, S. E.,
    9. Metcalf, D. and
    10. Nicola, N. A.
    (1998). Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Nat. Acad. Sci. USA 95, 114–119
    OpenUrlAbstract/FREE Full Text
    1. Hilton, D. J.
    (1999). Negative regulators of cytokine signal transduction. Cell. Mol. Life Sci 55, 1568–1577
    OpenUrlCrossRefPubMedWeb of Science
    1. Isaksen, D. E.,
    2. Baumann, H.,
    3. Trobridge, P. A.,
    4. Farr, A. G.,
    5. Levin, S. D. and
    6. Ziegler, S. F.
    (1999). Requirement for Stat5 in thymic stromal lymphopoietin-mediated signal transduction. J. Immunol 163, 5971–5977
    OpenUrlAbstract/FREE Full Text
    1. Ito, S.,
    2. Ansari, P.,
    3. Sakatsume, M.,
    4. Dickensheets, H.,
    5. Vazquez, N.,
    6. Donnelly, R. P.,
    7. Larner, A. C. and
    8. Finbloom, D. S.
    (1999). Interleukin-10 inhibits expression of both interferon alpha-and interferon gamma-induced genes by suppressing tyrosine phosphorylation of STAT1. Blood 93, 1456–1463
    OpenUrlAbstract/FREE Full Text
    1. Kamura, T.,
    2. Sato, S.,
    3. Haque, D.,
    4. Liu, L.,
    5. Kaelin, W. G. Jr..,
    6. Conaway, R. C. and
    7. Conaway, J. W.
    (1998). The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families. Genes Dev 12, 3872–3881
    OpenUrlAbstract/FREE Full Text
    1. Klingmuller, U.,
    2. Bergelson, S.,
    3. Hsiao, J. G. and
    4. Lodish, H. F.
    (1996). Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5. Proc. Nat. Acad. Sci. USA 93, 8324–8328
    OpenUrlAbstract/FREE Full Text
    1. Losman, J. A.,
    2. Chen, X. P.,
    3. Hilton, D. J. and
    4. Rothman, P.
    (1999). SOCS-1 is a potent inhibitor of IL-4 signal transduction. J. Immunol 162, 3770–3774
    OpenUrlAbstract/FREE Full Text
    1. Marine, J. C.,
    2. Topham, D. J.,
    3. McKay, C.,
    4. Wang, D.,
    5. Parganas, E.,
    6. Stravopodis, D.,
    7. Yoshimura, A. and
    8. Ihle, J. N.
    (1999). SOCS1 deficiency causes a lymphocyte-dependent perinatal lethality. Cell 98, 609–616
    OpenUrlCrossRefPubMedWeb of Science
    1. Marine, J. C.,
    2. McKay, C.,
    3. Wang, D.,
    4. Topham, D. J.,
    5. Parganas, E.,
    6. Nakajima, H.,
    7. Pendeville, H.,
    8. Yasukawa, H.,
    9. Sasaki, A.,
    10. Yoshimura, A. and
    11. Ihle, J. N.
    (1999). SOCS3 is essential in the regulation of fetal liver erythropoiesis. Cell 98, 617–627
    OpenUrlCrossRefPubMedWeb of Science
    1. Masuhara, M.,
    2. Sakamoto, H.,
    3. Matsumoto, A.,
    4. Suzuki, R.,
    5. Yasukawa, H.,
    6. Mitsui, K.,
    7. Wakioka, T.,
    8. Tanimura, S.,
    9. Sasaki, A.,
    10. Misawa, H.,
    11. Yokouchi, M.,
    12. Ohtsubo, M. and
    13. Yoshimura, A.
    (1997). Cloning and characterization of novel CIS family genes. Biochem. Biophys. Res. Commun 239, 439–446
    OpenUrlCrossRefPubMedWeb of Science
    1. Matsumoto, A.,
    2. Masuhara, M.,
    3. Mitsui, K.,
    4. Yokouchi, M.,
    5. Ohtsubo, M.,
    6. Misawa, H.,
    7. Miyajima, A. and
    8. Yoshimura, A.
    (1997). CIS, a cytokine inducible SH2 protein, is a target of the JAK-STAT5 pathway and modulates STAT5 activation. Blood 89, 3148–3154
    OpenUrlAbstract/FREE Full Text
    1. Matsumoto, A.,
    2. Seki, Y.,
    3. Kubo, M.,
    4. Ohtsuka, S.,
    5. Suzuki, A.,
    6. Hayashi, I.,
    7. Tsuji, K.,
    8. Nakahata, T.,
    9. Okabe, M.,
    10. Yamada, S. and
    11. Yoshimura, A.
    (1999). Suppression of STAT5 functions in liver, mammary glands, and T cells in cytokine-inducible SH2-containing protein 1 transgenic mice. Mol. Cell. Biol 19, 6396–6407
    OpenUrlAbstract/FREE Full Text
    1. Matuoka, K.,
    2. Miki, H.,
    3. Takahashi, K. and
    4. Takenawa, T.
    (1997). A novel ligand for an SH3 domain of the adaptor protein Nck bears an SH2 domain and nuclear signaling motifs. Biochem. Biophys. Res. Commun 239, 488–492
    OpenUrlCrossRefPubMedWeb of Science
    1. Minamoto, S.,
    2. Ikegame, K.,
    3. Ueno, K.,
    4. Narazaki, M.,
    5. Naka, T.,
    6. Yamamoto, H.,
    7. Matsumoto, T.,
    8. Saito, H.,
    9. Hosoe, S. and
    10. Kishimoto, T.
    (1997). Cloning and functional analysis of new members of STAT induced STAT inhibitor (SSI) family: SSI-2 and SSI-3. Biochem. Biophys. Res. Commun 237, 79–83
    OpenUrlCrossRefPubMedWeb of Science
    1. Mui, A. L.,
    2. Wakao, H.,
    3. Kinoshita, T.,
    4. Kitamura, T. and
    5. Miyajima, A.
    (1996). Suppression of interleukin-3-induced gene expression by a C-terminal truncated Stat5: role of Stat5 in proliferation. EMBO J 15, 2425–2433
    OpenUrlPubMedWeb of Science
    1. Naka, T.,
    2. Narazaki, M.,
    3. Hirata, M.,
    4. Matsumoto, T.,
    5. Minamoto, S.,
    6. Aono, A.,
    7. Nishimoto, N.,
    8. Kajita, T.,
    9. Taga, T.,
    10. Yoshizaki, K.,
    11. Akira, S. and
    12. Kishimoto, T.
    (1997). Structure and function of a new STAT-induced STAT inhibitor. Nature 387, 924–929
    OpenUrlCrossRefPubMedWeb of Science
    1. Naka, T.,
    2. Matsumoto, T.,
    3. Narazaki, M.,
    4. Fujimoto, M.,
    5. Morita, Y.,
    6. Ohsawa, Y.,
    7. Saito, H.,
    8. Nagasawa, T.,
    9. Uchiyama, Y. and
    10. Kishimoto, T.
    (1998). Accelerated apoptosis in lymphocytes by augmented induction of Bax in SSI-1 (STAT-induced STAT inhibitor-1) deficient mice. Proc. Nat. Acad. Sci. USA 95, 15577–15582
    OpenUrlAbstract/FREE Full Text
    1. Narazaki, M.,
    2. Fujimoto, M.,
    3. Matsumoto, T.,
    4. Morita, Y.,
    5. Saito, H.,
    6. Kajita, T.,
    7. Yoshizaki, K.,
    8. Naka, T. and
    9. Kishimoto, T.
    (1998). Three distinct domains of SSI-1/SOCS-1/JAB protein are required for its suppression of interleukin 6 signaling. Proc. Nat. Acad. Sci. USA 95, 13130–13134
    OpenUrlAbstract/FREE Full Text
    1. Neubauer, H.,
    2. Cumano, A.,
    3. Muller, M.,
    4. Wu, H.,
    5. Huffstadt, U. and
    6. Pfeffer, K.
    (1998). Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 93, 397–409
    OpenUrlCrossRefPubMedWeb of Science
    1. Nicholson, S. E.,
    2. Willson, T. A.,
    3. Farley, A.,
    4. Starr, R.,
    5. Zhang, J. G.,
    6. Baca, M.,
    7. Alexander, W. S.,
    8. Metcalf, D.,
    9. Hilton, D. J. and
    10. Nicola, N. A.
    (1999). Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIF and IL-6 signal transduction. EMBO J 18, 375–385
    OpenUrlAbstract
    1. Ohya, K.,
    2. Kajigaya, S.,
    3. Yamashita, Y.,
    4. Miyazato, A.,
    5. Hatake, K.,
    6. Miura, Y.,
    7. Ikeda, U.,
    8. Shimada, K.,
    9. Ozawa, K. and
    10. Mano, H.
    (1997). SOCS-1/JAB/SSI-1 can bind to and suppress Tec protein-tyrosine kinase. J. Biol. Chem 272, 27178–27182
    OpenUrlAbstract/FREE Full Text
    1. Parganas, E.,
    2. Wang, D.,
    3. Stravopodis, D.,
    4. Topham, D. J.,
    5. Marine, J. C.,
    6. Teglund, S.,
    7. Vanin, E. F.,
    8. Bodner, S.,
    9. Colamonici, O. R.,
    10. van Deursen, J. M.,
    11. Grosveld, G. and
    12. Ihle, J. N.
    (1998). Jak2 is essential for signaling through a variety of cytokine receptors. Cell 93, 385–395
    OpenUrlCrossRefPubMedWeb of Science
    1. Pezet, A.,
    2. Favre, H.,
    3. Kelly, P. A. and
    4. Edery, M.
    (1999). Inhibition and restoration of prolactin signal transduction by suppressors of cytokine signaling. J. Biol. Chem 274, 24497–24502
    OpenUrlAbstract/FREE Full Text
    1. Ram, P. A. and
    2. Waxman, D. J.
    (1999). SOCS/CIS protein inhibition of growth hormone-stimulated STAT5 signaling by multiple mechanisms. J. Biol. Chem 274, 35553–35561
    OpenUrlAbstract/FREE Full Text
    1. Song, M. M. and
    2. Shuai, K.
    (1998). The suppressor of cytokine signaling (SOCS) 1 and SOCS3 but not SOCS2 proteins inhibit interferon-mediated antiviral and antiproliferative activities. J. Biol. Chem 273, 35056–35062
    OpenUrlAbstract/FREE Full Text
    1. Starr, R.,
    2. Willson, T. A.,
    3. Viney, E. M.,
    4. Murray, L. J.,
    5. Rayner, J. R.,
    6. Jenkins, B. J.,
    7. Gonda, T. J.,
    8. Alexander, W. S.,
    9. Metcalf, D.,
    10. Nicola, N. A. and
    11. Hilton, D. J.
    (1997). A family of cytokine-inducible inhibitors of signalling. Nature 387, 917–921
    OpenUrlCrossRefPubMedWeb of Science
    1. Starr, R.,
    2. Metcalf, D.,
    3. Elefanty, A. G.,
    4. Brysha, M.,
    5. Willson, T. A.,
    6. Nicola, N. A.,
    7. Hilton, D. J. and
    8. Alexander, W. S.
    (1998). Liver degeneration and lymphoid deficiencies in mice lacking suppressor of cytokine signaling-1. Proc. Nat. Acad. Sci. USA 95, 14395–14399
    OpenUrlAbstract/FREE Full Text
    1. Stoiber, D.,
    2. Kovarik, P.,
    3. Cohney, S.,
    4. Johnston, J. A.,
    5. Steinlein, P. and
    6. Decker, T.
    (1999). Lipopolysaccharide induces in macrophages the synthesis of the suppressor of cytokine signaling 3 and suppresses signal transduction in response to the activating factor IFN-gamma. J. Immunol 163, 2640–2647
    OpenUrlAbstract/FREE Full Text
    1. Suzuki, R.,
    2. Sakamoto, H.,
    3. Yasukawa, H.,
    4. Masuhara, M.,
    5. Wakioka, T.,
    6. Sasaki, A.,
    7. Yuge, K.,
    8. Komiya, S.,
    9. Inoue, A. and
    10. Yoshimura, A.
    (1998). CIS3 and JAB have different regulatory roles in interleukin-6 mediated differentiation and STAT3 activation in M1 leukemia cells. Oncogene 17, 2271–2278
    OpenUrlCrossRefPubMedWeb of Science
    1. Teglund, S.,
    2. McKay, C.,
    3. Schuetz, E.,
    4. van Deursen, J. M.,
    5. Stravopodis, D.,
    6. Wang, D.,
    7. Brown, M.,
    8. Bodner, S.,
    9. Grosveld, G. and
    10. Ihle, J. N.
    (1998). Stat5a and Stat5b proteins have essential and nonessential, or redundant, roles in cytokine responses. Cell 93, 841–50
    OpenUrlCrossRefPubMedWeb of Science
    1. Vasiliauskas, D.,
    2. Hancock, S. and
    3. Stern, C. D.
    (1999). SWiP-1: novel SOCS box containing WD-protein regulated by signalling centres and by Shh during development. Mech. Dev 82, 79–94
    OpenUrlCrossRefPubMedWeb of Science
    1. Verdier, F.,
    2. Chretien, S.,
    3. Muller, O.,
    4. Varlet, P.,
    5. Yoshimura, A.,
    6. Gisselbrecht, S.,
    7. Lacombe, C. and
    8. Mayeux, P.
    (1998). Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein. J. Biol. Chem 273, 28185–28190
    OpenUrlAbstract/FREE Full Text
    1. Yasukawa, H.,
    2. Misawa, H.,
    3. Sakamoto, H.,
    4. Masuhara, M.,
    5. Sasaki, A.,
    6. Wakioka, T.,
    7. Ohtsuka, S.,
    8. Imaizumi, T.,
    9. Matsuda, T.,
    10. Ihle, J. N. and
    11. Yoshimura, A.
    (1999). The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop. EMBO J 18, 1309–1320
    OpenUrlAbstract
    1. Yoshimura, A.,
    2. Ohkubo, T.,
    3. Kiguchi, T.,
    4. Jenkins, N. A.,
    5. Gilbert, D. J.,
    6. Copeland, N. G.,
    7. Hara, T. and
    8. Miyajima, A.
    (1995). A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. EMBO J 14, 2816–2826
    OpenUrlPubMedWeb of Science
    1. Yu, C. and
    2. Burakoff, S. J.
    (1997). Involvement of proteasomes in regulating Jak-STAT pathways upon interleukin-2 stimulation. J. Biol. Chem 272, 14017–14020
    OpenUrlAbstract/FREE Full Text
    1. Zhang, J. G.,
    2. Farley, A.,
    3. Nicholson, S. E.,
    4. Willson, T. A.,
    5. Zugaro, L. M.,
    6. Simpson, R. J.,
    7. Moritz, R. L.,
    8. Cary, D.,
    9. Richardson, R.,
    10. Hausmann, G.,
    11. Kile, B. J.,
    12. Kent, S. B.,
    13. Alexander, W. S.,
    14. Metcalf, D.,
    15. Hilton, D. J.,
    16. Nicola, N. A. and
    17. Baca, M.
    (1999). The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation. Proc. Nat. Acad. Sci. USA 96, 2071–2076
    OpenUrlAbstract/FREE Full Text
Back to top

 Download PDF

Email
Journal Article
SOCS: physiological suppressors of cytokine signaling
D.L. Krebs, D.J. Hilton
Journal of Cell Science 2000 113: 2813-2819;
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
Citation Tools
Alerts

Article navigation

Other journals from The Company of Biologists

Advertisement

2020 at The Company of Biologists

Despite the challenges of 2020, we were able to bring a number of long-term projects and new ventures to fruition. While we look forward to a new year, join us as we reflect on the triumphs of the last 12 months.

Mole – The Corona Files

"This is not going to go away, 'like a miracle.' We have to do magic. And I know we can."

Mole continues to offer his wise words to researchers on how to manage during the COVID-19 pandemic.

Cell scientist to watch – Christine Faulkner

In an interview, Christine Faulkner talks about where her interest in plant science began, how she found the transition between Australia and the UK, and shares her thoughts on virtual conferences.

Read & Publish participation extends worldwide

“The clear advantages are rapid and efficient exposure and easy access to my article around the world. I believe it is great to have this publishing option in fast-growing fields in biomedical research.”

Dr Jaceques Behmoaras (Imperial College London) shares his experience of publishing Open Access as part of our growing Read & Publish initiative. We now have over 60 institutions in 12 countries taking part – find out more and view our full list of participating institutions.

JCS and COVID-19

For more information on measures Journal of Cell Science is taking to support the community during the COVID-19 pandemic, please see here.

If you have any questions or concerns, please do not hestiate to contact the Editorial Office.