Skip to main content
Advertisement

Main menu

  • Home
  • Articles
    • Accepted manuscripts
    • Issue in progress
    • Latest complete issue
    • Issue archive
    • Archive by article type
    • Special issues
    • Subject collections
    • Cell Scientists to Watch
    • First Person
    • Sign up for alerts
  • About us
    • About JCS
    • Editors and Board
    • Editor biographies
    • Travelling Fellowships
    • Grants and funding
    • Journal Meetings
    • Workshops
    • The Company of Biologists
    • Journal news
  • For authors
    • Submit a manuscript
    • Aims and scope
    • Presubmission enquiries
    • Fast-track manuscripts
    • Article types
    • Manuscript preparation
    • Cover suggestions
    • Editorial process
    • Promoting your paper
    • Open Access
    • JCS Prize
    • Manuscript transfer network
    • Biology Open transfer
  • Journal info
    • Journal policies
    • Rights and permissions
    • Media policies
    • Reviewer guide
    • Sign up for alerts
  • Contacts
    • Contact JCS
    • Subscriptions
    • Advertising
    • Feedback
    • For library administrators
  • COB
    • About The Company of Biologists
    • Development
    • Journal of Cell Science
    • Journal of Experimental Biology
    • Disease Models & Mechanisms
    • Biology Open

User menu

  • Log in
  • Log out

Search

  • Advanced search
Journal of Cell Science
  • COB
    • About The Company of Biologists
    • Development
    • Journal of Cell Science
    • Journal of Experimental Biology
    • Disease Models & Mechanisms
    • Biology Open

supporting biologistsinspiring biology

Journal of Cell Science

  • Log in
Advanced search

RSS   Twitter  Facebook   YouTube  

  • Home
  • Articles
    • Accepted manuscripts
    • Issue in progress
    • Latest complete issue
    • Issue archive
    • Archive by article type
    • Special issues
    • Subject collections
    • Cell Scientists to Watch
    • First Person
    • Sign up for alerts
  • About us
    • About JCS
    • Editors and Board
    • Editor biographies
    • Travelling Fellowships
    • Grants and funding
    • Journal Meetings
    • Workshops
    • The Company of Biologists
    • Journal news
  • For authors
    • Submit a manuscript
    • Aims and scope
    • Presubmission enquiries
    • Fast-track manuscripts
    • Article types
    • Manuscript preparation
    • Cover suggestions
    • Editorial process
    • Promoting your paper
    • Open Access
    • JCS Prize
    • Manuscript transfer network
    • Biology Open transfer
  • Journal info
    • Journal policies
    • Rights and permissions
    • Media policies
    • Reviewer guide
    • Sign up for alerts
  • Contacts
    • Contact JCS
    • Subscriptions
    • Advertising
    • Feedback
    • For library administrators
Journal Articles
A cdc2-like kinase distinct from cdk5 is associated with neurofilaments
R. Starr, F.L. Hall, M.J. Monteiro
Journal of Cell Science 1996 109: 1565-1573;
R. Starr
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
F.L. Hall
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
M.J. Monteiro
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Info & metrics
  • PDF
Loading

Summary

An immunoprecipitation assay was used to identify protein kinases which are physically associated with neurofilaments (NF) in mouse brain extracts. Using this approach, we show that a cdc2-related kinase is associated with NF. The cdc2-related kinase was found to be distinct from cdk5 and the authentic cdc2 by a number of criteria. Firstly, it has a molecular mass on SDS-PAGE gels of 34 kDa, similar to that of cdc2, but differing from cdk5 (31 kDa). Secondly, it is not recognized by an antibody specific for cdk5. Thirdly, it is recognized by an antibody raised against the C-terminal region of authentic cdc2, but not by an antibody specific for the PSTAIRE motif. Using immunoblotting, we further show that the cdc2-related kinase copurifies with NF isolated from rat tissues. In vitro kinase assays further demonstrated that immunoprecipitated cdc2-related kinase phosphorylates recombinant NF-H protein. Phosphorylation of NF-H by the cdc2-like activity was not affected by 3 microM olomoucine but was inhibited by 10 microM of this kinase inhibitor. Phosphoamino acid analysis of in vitro phosphorylated NF-H indicates that the immunoprecipitated cdc2-related kinase phosphorylates serine residues.

  • © 1996 by Company of Biologists

REFERENCES

    1. Atherton-Fessler S.,
    2. Liu F.,
    3. Gabrielli B.,
    4. Lee M. S.,
    5. Peng C.-Y. and
    6. Piwnica-Worms H.
    (1994). Cell cycle regulation of the p34cdc2inhibitory kinases. Mol. Biol. Cell 5, 989–1001
    OpenUrlAbstract/FREE Full Text
    1. Barbacid M.,
    2. Lamballe F.,
    3. Pulido D. and
    4. Klein R.
    (1991). The trk family of tyrosine protein kinase receptors. Biochim. Biophys. Acta 1072, 115–127
    OpenUrlPubMed
    1. Benfenati F.,
    2. Valtorta F.,
    3. Rubenstein J. L.,
    4. Gorelick F. S.,
    5. Greengard P. and
    6. Czernik A. J.
    (1992). Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. Nature 359, 417–420
    OpenUrlCrossRefPubMedWeb of Science
    1. Carden M. J.,
    2. Trojanowski J. Q.,
    3. Schlaepfer W. W. and
    4. Lee V. M.-Y.
    (1987). Two stage expression of neurofilament polypeptides during rat neurogenesis with early establishment of adult phosphorylation patterns. J. Neurosci 7, 3489–3504
    OpenUrlAbstract
    1. Cobb M. H.,
    2. Helper J. E.,
    3. Cheng M. and
    4. Robbins D.
    (1994). The mitogen-activated protein kinases, ERK1 and ERK2. Semin. Cancer Biol 5, 261–268
    OpenUrlPubMedWeb of Science
    1. Cote F.,
    2. Collard J.-F. and
    3. Julien J.-P.
    (1993). Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell 73, 35–46
    OpenUrlCrossRefPubMedWeb of Science
    1. de Waegh S. M.,
    2. Lee V. M.-Y. and
    3. Brady S. T.
    (1992). Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell 68, 451–463
    OpenUrlCrossRefPubMedWeb of Science
    1. Dosemici A.,
    2. Floyd C. C. and
    3. Pant H. C.
    (1990). Characterization of neurofilament-associated protein kinase activities from bovine spinal cord. Cell. Mol. Neurobiol 10, 369–382
    OpenUrlCrossRefPubMedWeb of Science
    1. Eyer J. and
    2. Peterson A.
    (1994). Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament--galactosidase fusion protein. Neuron 12, 389–405
    OpenUrlCrossRefPubMedWeb of Science
    1. Fleigner K. H. and
    2. Liem R. K.
    (1991). Cellular and molecular biology of neuronal intermediate filaments. Int. Rev. Cytol 131, 109–167
    OpenUrlCrossRefPubMed
    1. Geisler N.,
    2. Vanderkerckhove J. and
    3. Weber K.
    (1987). Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H. FEBS Lett 221, 403–407
    OpenUrlCrossRefPubMedWeb of Science
    1. Grana X.,
    2. De Luca A.,
    3. Sang N.,
    4. Fu Y.,
    5. Claudio P. P.,
    6. Rosenblatt J.,
    7. Morgan D. O. and
    8. Giordano A.
    (1994). PITALRE, a nuclear CDC2-related protein kinase that phosphorylates the retinoblastoma protein in vitro. Proc. Nat. Acad. Sci. USA 91, 3834–3838
    OpenUrlAbstract/FREE Full Text
    1. Greengard P.,
    2. Valtorta F.,
    3. Czernik A. J. and
    4. Benfenati F.
    (1993). Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259, 780–785
    OpenUrlAbstract/FREE Full Text
    1. Guan R. J.,
    2. Hall F. L. and
    3. Cohlberg J. A.
    (1992). Proline-directed protein kinase (p34cdc2/p58cyclinA) phosphorylates bovine neurofilaments. J. Neurochem 58, 1365–1371
    OpenUrlCrossRefPubMed
    1. Hanks S. K.,
    2. Calalb M. B.,
    3. Harper M. C. and
    4. Patel S. K.
    (1992). Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Nat. Acad. Sci. USA 89, 8487–8491
    OpenUrlAbstract/FREE Full Text
    1. Hayes T. E.,
    2. Valtz N. L. M. and
    3. McKay R. D. G.
    (1991). Downregulation of cdc2 upon terminal differentiation of neurons. New Biol 3, 259–269
    OpenUrlPubMedWeb of Science
    1. Hellmich M. R.,
    2. Pant H. C.,
    3. Wada E. and
    4. Battey J. F.
    (1992). Neuronal cdc2-like kinase: A cdc2 related protein kinase with predominantly neuronal expression. Proc. Nat. Acad. Sci. USA 89, 10867–10871
    OpenUrlAbstract/FREE Full Text
    1. Hisanaga S.,
    2. Kusubata M.,
    3. Okumura E. and
    4. Kishimoto T.
    (1991). Phosphorylation of neurofilament H subunit at the tail domain by cdc2 kinase dissociates the association to microtubules. J. Biol. Chem 266, 21798–21803
    OpenUrlAbstract/FREE Full Text
    1. Hisanaga S.,
    2. Ishiguro K.,
    3. Uchida T.,
    4. Okumura E.,
    5. Okana T. and
    6. Kishimoto T.
    (1993). Tau protein kinase II has a similar characteristic to cdc2 kinase for phosphorylating neurofilament proteins. J. Biol. Chem 268, 15056–15060
    OpenUrlAbstract/FREE Full Text
    1. Hsieh S. T.,
    2. Kidd G. J.,
    3. Crawford T. O.,
    4. Xu Z.,
    5. Lin W.-M.,
    6. Trapp B. D.,
    7. Cleveland D. W. and
    8. Griffin J. W.
    (1994). Regional modulation of neurofilament organization by myelination in normal axons. J. Neurosci 14, 6392–6401
    OpenUrlAbstract
    1. Julien J.-P. and
    2. Mushynski W. E.
    (1983). The distribution ofphosphorylation sites among identified proteolytic fragments of mammalian neurofilaments. J. Biol. Chem 258, 4019–4025
    OpenUrlAbstract/FREE Full Text
    1. Lee V. M.-Y.,
    2. Otvos L. Jr..,
    3. Carden M. J.,
    4. Hollosi M.,
    5. Dietzschold B. and
    6. Lazzarini R.
    (1988). Identification of the major multiphosphorylation site in mammalian neurofilaments. Proc. Nat. Acad. Sci. USA 85, 1998–2002
    OpenUrlAbstract/FREE Full Text
    1. Lew J.,
    2. Winkfein R. J.,
    3. Paudel H. K. and
    4. Wang J. H.
    (1992). Brain proline-directed protein kinase is a neurofilament kinase which displays high sequence homology to p34cdc2. J. Biol. Chem 267, 25922–25926
    OpenUrlAbstract/FREE Full Text
    1. Lew J.,
    2. Huang Q.-Q.,
    3. Qi Z.,
    4. Winkfein R. J.,
    5. Aebersold R.,
    6. Hunt T. and
    7. Wang J. H.
    (1994). A brain specific activator of cyclin-dependent kinase 5. Nature 371, 423–426
    OpenUrlCrossRefPubMed
    1. Lew J. and
    2. Wang J. H.
    (1995). Neuronal cdc2-like kinase. Trends Biochem. Sci 20, 33–37
    OpenUrlCrossRefPubMedWeb of Science
    1. Lewis S. E. and
    2. Nixon R. A.
    (1988). Multiple phosphorylated variants of the high molecular mass subunit of neurofilaments in axons of retinal cell neurons: Characterization and evidence for their differential association with stationary and moving neurofilaments. J. Cell Biol 107, 2689–2701
    OpenUrlAbstract/FREE Full Text
    1. Liu W.-K.,
    2. Williams R. T.,
    3. Hall F. L.,
    4. Dickson D. W. and
    5. Yen S.-H.
    (1995). Detection of a cdc2-related kinase associated with Alzheimer paired helical filament. Am. J. Pathol 146, 228–238
    OpenUrlPubMedWeb of Science
    1. Meyerson M.,
    2. Enders G. H.,
    3. Wu C.-L.,
    4. Su L.-K.,
    5. Gorka C.,
    6. Nelson C.,
    7. Harlow E. and
    8. Tsai L.-H.
    (1992). A family of human cdc2-related protein kinases. EMBO J 11, 2909–2917
    OpenUrlPubMedWeb of Science
    1. Monteiro M. J.,
    2. Hoffman P. N.,
    3. Gearhart J. D. and
    4. Cleveland D. W.
    (1990). Expression of neurofilament-L in both neuronal and non-neuronal cells of transgenic mice: increased neurofilament density in axons without affecting caliber. J. Cell Biol 111, 1543–1557
    OpenUrlAbstract/FREE Full Text
    1. Nixon R. A. and
    2. Sihag R. K.
    (1991). Neurofilament phosphorylation: a new look at regulation and function. Trends Neurosci 14, 501–505
    OpenUrlCrossRefPubMedWeb of Science
    1. Nixon R.
    (1993). The regulation of neurofilament protein dynamics by phosphorylation: clues to neurofibrillary pathobiology. Brain Pathol 3, 29–38
    OpenUrlCrossRefPubMedWeb of Science
    1. Nixon R. A.,
    2. Paskevich P. A.,
    3. Sihag R. K. and
    4. Thayer C. Y.
    (1994). Phosphorylation on carboxyl-terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: Influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber. J. Cell Biol 126, 1031–1046
    OpenUrlAbstract/FREE Full Text
    1. Nurse P.
    (1990). Universal control mechanism regulating onset of M-phase. Nature 344, 503–508
    OpenUrlCrossRefPubMedWeb of Science
    1. Ohara O.,
    2. Gahara Y.,
    3. Miyake T.,
    4. Teraoka H. and
    5. Kitamura T.
    (1993). Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene. J. Cell Biol 121, 387–395
    OpenUrlAbstract/FREE Full Text
    1. Peeper D. S.,
    2. Parker L. L.,
    3. Ewen M. E.,
    4. Toebes M.,
    5. Hall F. L.,
    6. Xu M.,
    7. Zantema A.,
    8. van der Eb A. J. and
    9. Piwnica-Worms H.
    (1993). A-and B-type cyclins differentially modulate substrate specificity of cyclin-cdk complexes. EMBO J 12, 1947–1954
    OpenUrlPubMedWeb of Science
    1. Pines J.
    (1993). Cyclins and cyclin-dependent kinases: take your partners. Trends Biochem. Sci 18, 195–197
    OpenUrlCrossRefPubMedWeb of Science
    1. Pines J. and
    2. Hunter T.
    (1989). Isolation of a human cyclin cDNA: Evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2. Cell 58, 833–846
    OpenUrlCrossRefPubMedWeb of Science
    1. Roder H. M. and
    2. Ingram V. M.
    (1991). Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichiometric ratios. J. Neurosci 11, 3325–3343
    OpenUrlAbstract
    1. Sakaguchi T.,
    2. Okada M.,
    3. Kitamura T. and
    4. Kawasaki K.
    (1993). Reduced diameter and conduction velocity of myelinated fibres in the sciatic nerve of a neurofilament-deficient mutant quail. Neurosci. Lett 153, 65–68
    OpenUrlCrossRefPubMedWeb of Science
    1. Shetty K. T.,
    2. Kaech S.,
    3. Link W. T.,
    4. Jaffe H.,
    5. Flores C. M.,
    6. Wray S.,
    7. Pant H. C. and
    8. Beushausen S.
    (1995). Molecular characterization of a neuronal-specific protein that stimulates the activity of cdk5. J. Neurochem 64, 1988–1995
    OpenUrlPubMedWeb of Science
    1. Sihag R. K.,
    2. Jeng A. Y. and
    3. Nixon R. A.
    (1988). Phosphorylation of neurofilament proteins by protein kinase C. FEBS Lett 233, 181–185
    OpenUrlCrossRefPubMedWeb of Science
    1. Soans C.,
    2. Holash J. A. and
    3. Pasquale E. B.
    (1994). Characterization of the expression of the Cek8 receptor-type tyrosine kinase during development and in tumor cell lines. Oncogene 9, 3353–3361
    OpenUrlPubMedWeb of Science
    1. Sternberger L. and
    2. Sternberger N.
    (1983). Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ. Proc. Nat. Acad. Sci.USA 80, 6126–6130
    OpenUrlAbstract/FREE Full Text
    1. Starr R.,
    2. Xiao J. and
    3. Monteiro M. J.
    (1995). Production of monoclonal antibodies against neurofilament-associated proteins: Demonstration of association with neurofilaments by a coimmunoprecipitation method. J. Neurochem 64, 1860–1867
    OpenUrlPubMed
    1. Tsai L.-H.,
    2. Takahashi T.,
    3. Caviness V. S. Jr.. and
    4. Harlow E.
    (1993). Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system. Development 119, 1029–1040
    OpenUrlAbstract
    1. Tsai L.-H.,
    2. Delalle I.,
    3. Caviness V. S. Jr..,
    4. Chae T. and
    5. Harlow E.
    (1994). p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5. Nature 371, 419–423
    OpenUrlCrossRefPubMed
    1. Vallano M. L.,
    2. Buckholz T. M. and
    3. DeLorenzo R. J.
    (1985). Phosphorylation of neurofilament proteins by endogenous calcium/calmodulin-dependent protein kinase. Biochem. Biophys. Res. Commun 130, 957–963
    OpenUrlCrossRefPubMed
    1. Vesely J.,
    2. Havlicek L.,
    3. Strnad M.,
    4. Blow J. J.,
    5. Donella-Deana A.,
    6. Pinna L.,
    7. Letham D. S.,
    8. Kato J.-Y.,
    9. Detivaud L.,
    10. Leclerc S. and
    11. Meijer L.
    (1994). Inhibition of cyclin-dependent kinases by purine analogues. Eur. J. Biochem 224, 771–786
    OpenUrlCrossRefPubMedWeb of Science
    1. Wible B. A.,
    2. Smith K. E. and
    3. Angelides K. J.
    (1989). Resolution and purification of a neurofilament-specific kinase. Proc. Nat. Acad. Sci. USA 86, 720–724
    OpenUrlAbstract/FREE Full Text
    1. Williams R.,
    2. Sanghera J.,
    3. Wu F.,
    4. Carbonaro-Hall D.,
    5. Campbell D. L.,
    6. Warburton D.,
    7. Pelech S. and
    8. Hall F.
    (1993). Identification of a human epidermal growth factor receptor-associated protein kinase as a new member of the mitogen-activated protein kinase/extracellular signal-regulated protein kinase family. J. Biol. Chem 268, 18213–18217
    OpenUrlAbstract/FREE Full Text
    1. Xiao J. and
    2. Monteiro M. J.
    (1994). Identification and characterization of a novel (115kDa) neurofilament-associated kinase. J. Neurosci 14, 1820–1833
    OpenUrlAbstract
    1. Xiong Y.,
    2. Zhang H. and
    3. Beach D.
    (1992). D-type cyclins associate with multiple protein kinases and the DNA replication and repair factor PCNA. Cell 71, 505–514
    OpenUrlCrossRefPubMedWeb of Science
    1. Xu Z.,
    2. Cork L. C.,
    3. Griffin J. W. and
    4. Cleveland D. W.
    (1993). Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell 73, 23–33
    OpenUrlCrossRefPubMedWeb of Science
    1. Xu Z.,
    2. Dong D. L. Y. and
    3. Cleveland D. W.
    (1994). Neuronal intermediate filaments: new progress on an old subject. Curr. Opin. Neurobiol 4, 655–661
    OpenUrlCrossRefPubMed
    1. Yamasaki H.,
    2. Bennett G.,
    3. Itakura C. and
    4. Mizutani M.
    (1992). Defective expression of neurofilament protein subunits in hereditary hypotrophic axonopathy of quail. Lab. Invest 66, 734–743
    OpenUrlPubMedWeb of Science
Previous ArticleNext Article
Back to top
Previous ArticleNext Article

This Issue

 Download PDF

Email

Thank you for your interest in spreading the word on Journal of Cell Science.

NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.

Enter multiple addresses on separate lines or separate them with commas.
A cdc2-like kinase distinct from cdk5 is associated with neurofilaments
(Your Name) has sent you a message from Journal of Cell Science
(Your Name) thought you would like to see the Journal of Cell Science web site.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Journal Articles
A cdc2-like kinase distinct from cdk5 is associated with neurofilaments
R. Starr, F.L. Hall, M.J. Monteiro
Journal of Cell Science 1996 109: 1565-1573;
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
Citation Tools
Journal Articles
A cdc2-like kinase distinct from cdk5 is associated with neurofilaments
R. Starr, F.L. Hall, M.J. Monteiro
Journal of Cell Science 1996 109: 1565-1573;

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Alerts

Please log in to add an alert for this article.

Sign in to email alerts with your email address

Article navigation

  • Top
  • Article
  • Info & metrics
  • PDF

Related articles

Cited by...

More in this TOC section

  • Involvement of actin filaments and integrins in the binding step in collagen phagocytosis by human fibroblasts
  • University administration
  • The cytoplasmic domain of the interleukin-6 receptor gp80 mediates its basolateral sorting in polarized madin-darby canine kidney cells
Show more Journal Articles

Similar articles

Other journals from The Company of Biologists

Development

Journal of Experimental Biology

Disease Models & Mechanisms

Biology Open

Advertisement

Cell scientist to watch: Janet Iwasa

Read our interview with molecular animator Janet Iwasa, where she talks about her transition from the wet lab, explains how animation can facilitate research and discusses the challenges of the field.


New funding scheme supports sustainable events

As part of our Sustainable Conferencing Initiative, we are pleased to announce funding for organisers that seek to reduce the environmental footprint of their event. The next deadline to apply for a Scientific Meeting grant is 26 March 2021.


Mole – The Corona files

“Despite everything, it's just incredible that we get to do science.”

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


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.

Articles

  • Accepted manuscripts
  • Issue in progress
  • Latest complete issue
  • Issue archive
  • Archive by article type
  • Special issues
  • Subject collections
  • Interviews
  • Sign up for alerts

About us

  • About Journal of Cell Science
  • Editors and Board
  • Editor biographies
  • Travelling Fellowships
  • Grants and funding
  • Journal Meetings
  • Workshops
  • The Company of Biologists

For Authors

  • Submit a manuscript
  • Aims and scope
  • Presubmission enquiries
  • Fast-track manuscripts
  • Article types
  • Manuscript preparation
  • Cover suggestions
  • Editorial process
  • Promoting your paper
  • Open Access
  • JCS Prize
  • Manuscript transfer network
  • Biology Open transfer

Journal Info

  • Journal policies
  • Rights and permissions
  • Media policies
  • Reviewer guide
  • Sign up for alerts

Contacts

  • Contact JCS
  • Subscriptions
  • Advertising
  • Feedback

Twitter   YouTube   LinkedIn

© 2021   The Company of Biologists Ltd   Registered Charity 277992