Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1990 Nov 1;111(5):1971–1985. doi: 10.1083/jcb.111.5.1971

Assembly of amino-terminally deleted desmin in vimentin-free cells

PMCID: PMC2116339  PMID: 1699950

Abstract

To study the role of the amino-terminal domain of the desmin subunit in intermediate filament (IF) formation, several deletions in the sequence encoding this domain were made. The deleted hamster desmin genes were fused to the RSV promoter. Expression of such constructs in vimentin- free MCF-7 cells as well as in vimentin-containing HeLa cells, resulted in the synthesis of mutant proteins of the expected size. Single- and double-label immunofluorescence assays of transfected cells showed that in the absence of vimentin, desmin subunits missing amino acids 4-13 are still capable of filament formation, although in addition to filaments large numbers of desmin dots are present. Mutant desmin subunits missing larger portions of their amino terminus cannot form filaments on their own. It may be concluded that the amino-terminal region comprising amino acids 7-17 contains residues indispensable for desmin filament formation in vivo. Furthermore it was shown that the endogenous vimentin IF network in HeLa cells masks the effects of mutant desmin on IF assembly. Intact and mutant desmin colocalized completely with endogenous vimentin in HeLa cells. Surprisingly, in these cells endogenous keratin also seemed to colocalize with endogenous vimentin, even if the endogenous vimentin filaments were disturbed after expression of some of the mutant desmin proteins. In MCF-7 cells some overlap between endogenous keratin and intact exogenous desmin filaments was also observed, but mutant desmin proteins did not affect the keratin IF structures. In the absence of vimentin networks (MCF-7 cells), the initiation of desmin filament formation seems to start on the preexisting keratin filaments. However, in the presence of vimentin (HeLa cells) a gradual integration of desmin in the preexisting vimentin filaments apparently takes place.

Full Text

The Full Text of this article is available as a PDF (5.6 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Albers K., Fuchs E. Expression of mutant keratin cDNAs in epithelial cells reveals possible mechanisms for initiation and assembly of intermediate filaments. J Cell Biol. 1989 Apr;108(4):1477–1493. doi: 10.1083/jcb.108.4.1477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Albers K., Fuchs E. The expression of mutant epidermal keratin cDNAs transfected in simple epithelial and squamous cell carcinoma lines. J Cell Biol. 1987 Aug;105(2):791–806. doi: 10.1083/jcb.105.2.791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ando S., Tanabe K., Gonda Y., Sato C., Inagaki M. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry. 1989 Apr 4;28(7):2974–2979. doi: 10.1021/bi00433a035. [DOI] [PubMed] [Google Scholar]
  4. Angelides K. J., Smith K. E., Takeda M. Assembly and exchange of intermediate filament proteins of neurons: neurofilaments are dynamic structures. J Cell Biol. 1989 Apr;108(4):1495–1506. doi: 10.1083/jcb.108.4.1495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bader B. L., Jahn L., Franke W. W. Low level expression of cytokeratins 8, 18 and 19 in vascular smooth muscle cells of human umbilical cord and in cultured cells derived therefrom, with an analysis of the chromosomal locus containing the cytokeratin 19 gene. Eur J Cell Biol. 1988 Dec;47(2):300–319. [PubMed] [Google Scholar]
  6. Bader B. L., Magin T. M., Hatzfeld M., Franke W. W. Amino acid sequence and gene organization of cytokeratin no. 19, an exceptional tail-less intermediate filament protein. EMBO J. 1986 Aug;5(8):1865–1875. doi: 10.1002/j.1460-2075.1986.tb04438.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Banks-Schlegel S. P., Harris C. C. Tissue-specific expression of keratin proteins in human esophageal and epidermal epithelium and their cultured keratinocytes. Exp Cell Res. 1983 Jul;146(2):271–280. doi: 10.1016/0014-4827(83)90129-5. [DOI] [PubMed] [Google Scholar]
  8. Bloemendal H., Pieper F. R. Intermediate filaments: known structure, unknown function. Biochim Biophys Acta. 1989 Apr 12;1007(3):245–253. doi: 10.1016/0167-4781(89)90144-9. [DOI] [PubMed] [Google Scholar]
  9. Broers J. L., Carney D. N., Klein Rot M., Schaart G., Lane E. B., Vooijs G. P., Ramaekers F. C. Intermediate filament proteins in classic and variant types of small cell lung carcinoma cell lines: a biochemical and immunochemical analysis using a panel of monoclonal and polyclonal antibodies. J Cell Sci. 1986 Jul;83:37–60. doi: 10.1242/jcs.83.1.37. [DOI] [PubMed] [Google Scholar]
  10. Capetanaki Y., Smith S., Heath J. P. Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation. J Cell Biol. 1989 Oct;109(4 Pt 1):1653–1664. doi: 10.1083/jcb.109.4.1653. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Capetanaki Y., Starnes S., Smith S. Expression of the chicken vimentin gene in transgenic mice: efficient assembly of the avian protein into the cytoskeleton. Proc Natl Acad Sci U S A. 1989 Jul;86(13):4882–4886. doi: 10.1073/pnas.86.13.4882. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Celis J. E., Larsen P. M., Fey S. J., Celis A. Phosphorylation of keratin and vimentin polypeptides in normal and transformed mitotic human epithelial amnion cells: behavior of keratin and vimentin filaments during mitosis. J Cell Biol. 1983 Nov;97(5 Pt 1):1429–1434. doi: 10.1083/jcb.97.5.1429. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Chou Y. H., Rosevear E., Goldman R. D. Phosphorylation and disassembly of intermediate filaments in mitotic cells. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1885–1889. doi: 10.1073/pnas.86.6.1885. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Domenjoud L., Jorcano J. L., Breuer B., Alonso A. Synthesis and fate of keratins 8 and 18 in nonepithelial cells transfected with cDNA. Exp Cell Res. 1988 Dec;179(2):352–361. doi: 10.1016/0014-4827(88)90274-1. [DOI] [PubMed] [Google Scholar]
  15. Evans R. M. Phosphorylation of vimentin in mitotically selected cells. In vitro cyclic AMP-independent kinase and calcium-stimulated phosphatase activities. J Cell Biol. 1989 Jan;108(1):67–78. doi: 10.1083/jcb.108.1.67. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Evans R. M. The intermediate-filament proteins vimentin and desmin are phosphorylated in specific domains. Eur J Cell Biol. 1988 Apr;46(1):152–160. [PubMed] [Google Scholar]
  17. Franke W. W. Nuclear lamins and cytoplasmic intermediate filament proteins: a growing multigene family. Cell. 1987 Jan 16;48(1):3–4. doi: 10.1016/0092-8674(87)90345-x. [DOI] [PubMed] [Google Scholar]
  18. Franke W. W., Schmid E., Mittnacht S., Grund C., Jorcano J. L. Integration of different keratins into the same filament system after microinjection of mRNA for epidermal keratins into kidney epithelial cells. Cell. 1984 Apr;36(4):813–825. doi: 10.1016/0092-8674(84)90031-x. [DOI] [PubMed] [Google Scholar]
  19. Geisler N., Hatzfeld M., Weber K. Phosphorylation in vitro of vimentin by protein kinases A and C is restricted to the head domain. Identification of the phosphoserine sites and their influence on filament formation. Eur J Biochem. 1989 Aug 1;183(2):441–447. doi: 10.1111/j.1432-1033.1989.tb14947.x. [DOI] [PubMed] [Google Scholar]
  20. Geisler N., Weber K. Phosphorylation of desmin in vitro inhibits formation of intermediate filaments; identification of three kinase A sites in the aminoterminal head domain. EMBO J. 1988 Jan;7(1):15–20. doi: 10.1002/j.1460-2075.1988.tb02778.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Geisler N., Weber K. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J. 1982;1(12):1649–1656. doi: 10.1002/j.1460-2075.1982.tb01368.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Georgatos S. D., Blobel G. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J Cell Biol. 1987 Jul;105(1):117–125. doi: 10.1083/jcb.105.1.117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Georgatos S. D., Blobel G. Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: a basis for a vectorial assembly of intermediate filaments. J Cell Biol. 1987 Jul;105(1):105–115. doi: 10.1083/jcb.105.1.105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Georgatos S. D., Marchesi V. T. The binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filament-membrane interactions. J Cell Biol. 1985 Jun;100(6):1955–1961. doi: 10.1083/jcb.100.6.1955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Georgatos S. D., Weaver D. C., Marchesi V. T. Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains. J Cell Biol. 1985 Jun;100(6):1962–1967. doi: 10.1083/jcb.100.6.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Georgatos S. D., Weber K., Geisler N., Blobel G. Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6780–6784. doi: 10.1073/pnas.84.19.6780. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Giudice G. J., Fuchs E. The transfection of epidermal keratin genes into fibroblasts and simple epithelial cells: evidence for inducing a type I keratin by a type II gene. Cell. 1987 Feb 13;48(3):453–463. doi: 10.1016/0092-8674(87)90196-6. [DOI] [PubMed] [Google Scholar]
  28. Glass C., Fuchs E. Isolation, sequence, and differential expression of a human K7 gene in simple epithelial cells. J Cell Biol. 1988 Oct;107(4):1337–1350. doi: 10.1083/jcb.107.4.1337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Gorman C. M., Merlino G. T., Willingham M. C., Pastan I., Howard B. H. The Rous sarcoma virus long terminal repeat is a strong promoter when introduced into a variety of eukaryotic cells by DNA-mediated transfection. Proc Natl Acad Sci U S A. 1982 Nov;79(22):6777–6781. doi: 10.1073/pnas.79.22.6777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Hattori M., Sakaki Y. Dideoxy sequencing method using denatured plasmid templates. Anal Biochem. 1986 Feb 1;152(2):232–238. doi: 10.1016/0003-2697(86)90403-3. [DOI] [PubMed] [Google Scholar]
  31. Herrmann H., Fouquet B., Franke W. W. Expression of intermediate filament proteins during development of Xenopus laevis. II. Identification and molecular characterization of desmin. Development. 1989 Feb;105(2):299–307. doi: 10.1242/dev.105.2.299. [DOI] [PubMed] [Google Scholar]
  32. Heuijerjans J. H., Pieper F. R., Ramaekers F. C., Timmermans L. J., Kuijpers H., Bloemendal H., Van Venrooij W. J. Association of mRNA and eIF-2 alpha with the cytoskeleton in cells lacking vimentin. Exp Cell Res. 1989 Apr;181(2):317–330. doi: 10.1016/0014-4827(89)90091-8. [DOI] [PubMed] [Google Scholar]
  33. Inagaki M., Gonda Y., Matsuyama M., Nishizawa K., Nishi Y., Sato C. Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin. J Biol Chem. 1988 Apr 25;263(12):5970–5978. [PubMed] [Google Scholar]
  34. Inagaki M., Nishi Y., Nishizawa K., Matsuyama M., Sato C. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature. 1987 Aug 13;328(6131):649–652. doi: 10.1038/328649a0. [DOI] [PubMed] [Google Scholar]
  35. Kaufmann E., Weber K., Geisler N. Intermediate filament forming ability of desmin derivatives lacking either the amino-terminal 67 or the carboxy-terminal 27 residues. J Mol Biol. 1985 Oct 20;185(4):733–742. doi: 10.1016/0022-2836(85)90058-0. [DOI] [PubMed] [Google Scholar]
  36. Kitamura S., Ando S., Shibata M., Tanabe K., Sato C., Inagaki M. Protein kinase C phosphorylation of desmin at four serine residues within the non-alpha-helical head domain. J Biol Chem. 1989 Apr 5;264(10):5674–5678. [PubMed] [Google Scholar]
  37. Knapp L. W., Bunn C. L. The experimental manipulation of keratin expression and organization in epithelial cells and somatic cell hybrids. Curr Top Dev Biol. 1987;22:69–96. doi: 10.1016/s0070-2153(08)60099-x. [DOI] [PubMed] [Google Scholar]
  38. Krimpenfort P. J., Schaart G., Pieper F. R., Ramaekers F. C., Cuypers H. T., van den Heuvel R. M., Vree Egberts W. T., van Eys G. J., Berns A., Bloemendal H. Tissue-specific expression of a vimentin--desmin hybrid gene in transgenic mice. EMBO J. 1988 Apr;7(4):941–947. doi: 10.1002/j.1460-2075.1988.tb02899.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Kulesh D. A., Ceceña G., Darmon Y. M., Vasseur M., Oshima R. G. Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8. Mol Cell Biol. 1989 Apr;9(4):1553–1565. doi: 10.1128/mcb.9.4.1553. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Lamb N. J., Fernandez A., Feramisco J. R., Welch W. J. Modulation of vimentin containing intermediate filament distribution and phosphorylation in living fibroblasts by the cAMP-dependent protein kinase. J Cell Biol. 1989 Jun;108(6):2409–2422. doi: 10.1083/jcb.108.6.2409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Lendahl U., Zimmerman L. B., McKay R. D. CNS stem cells express a new class of intermediate filament protein. Cell. 1990 Feb 23;60(4):585–595. doi: 10.1016/0092-8674(90)90662-x. [DOI] [PubMed] [Google Scholar]
  42. Li Z. L., Lilienbaum A., Butler-Browne G., Paulin D. Human desmin-coding gene: complete nucleotide sequence, characterization and regulation of expression during myogenesis and development. Gene. 1989 May 30;78(2):243–254. doi: 10.1016/0378-1119(89)90227-8. [DOI] [PubMed] [Google Scholar]
  43. Lippman M., Bolan G., Huff K. The effects of estrogens and antiestrogens on hormone-responsive human breast cancer in long-term tissue culture. Cancer Res. 1976 Dec;36(12):4595–4601. [PubMed] [Google Scholar]
  44. Loewinger L., McKeon F. Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm. EMBO J. 1988 Aug;7(8):2301–2309. doi: 10.1002/j.1460-2075.1988.tb03073.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Moll R., Franke W. W., Schiller D. L., Geiger B., Krepler R. The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells. Cell. 1982 Nov;31(1):11–24. doi: 10.1016/0092-8674(82)90400-7. [DOI] [PubMed] [Google Scholar]
  46. Monteiro M. J., Cleveland D. W. Expression of NF-L and NF-M in fibroblasts reveals coassembly of neurofilament and vimentin subunits. J Cell Biol. 1989 Feb;108(2):579–593. doi: 10.1083/jcb.108.2.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Nelson W. J., Traub P. Proteolysis of vimentin and desmin by the Ca2+-activated proteinase specific for these intermediate filament proteins. Mol Cell Biol. 1983 Jun;3(6):1146–1156. doi: 10.1128/mcb.3.6.1146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Ngai J., Coleman T. R., Lazarides E. Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly. Cell. 1990 Feb 9;60(3):415–427. doi: 10.1016/0092-8674(90)90593-4. [DOI] [PubMed] [Google Scholar]
  49. Pieper F. R., Schaart G., Krimpenfort P. J., Henderik J. B., Moshage H. J., van de Kemp A., Ramaekers F. C., Berns A., Bloemendal H. Transgenic expression of the muscle-specific intermediate filament protein desmin in nonmuscle cells. J Cell Biol. 1989 Mar;108(3):1009–1024. doi: 10.1083/jcb.108.3.1009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Quax-Jeuken Y. E., Quax W. J., Bloemendal H. Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence. Proc Natl Acad Sci U S A. 1983 Jun;80(12):3548–3552. doi: 10.1073/pnas.80.12.3548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Quax W., Egberts W. V., Hendriks W., Quax-Jeuken Y., Bloemendal H. The structure of the vimentin gene. Cell. 1983 Nov;35(1):215–223. doi: 10.1016/0092-8674(83)90224-6. [DOI] [PubMed] [Google Scholar]
  52. Quax W., van den Broek L., Egberts W. V., Ramaekers F., Bloemendal H. Characterization of the hamster desmin gene: expression and formation of desmin filaments in nonmuscle cells after gene transfer. Cell. 1985 Nov;43(1):327–338. doi: 10.1016/0092-8674(85)90038-8. [DOI] [PubMed] [Google Scholar]
  53. Quax W., van den Heuvel R., Egberts W. V., Quax-Jeuken Y., Bloemendal H. Intermediate filament cDNAs from BHK-21 cells: demonstration of distinct genes for desmin and vimentin in all vertebrate classes. Proc Natl Acad Sci U S A. 1984 Oct;81(19):5970–5974. doi: 10.1073/pnas.81.19.5970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Quinlan R. A., Franke W. W. Heteropolymer filaments of vimentin and desmin in vascular smooth muscle tissue and cultured baby hamster kidney cells demonstrated by chemical crosslinking. Proc Natl Acad Sci U S A. 1982 Jun;79(11):3452–3456. doi: 10.1073/pnas.79.11.3452. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Ramaekers F. C., Puts J. J., Moesker O., Kant A., Huysmans A., Haag D., Jap P. H., Herman C. J., Vooijs G. P. Antibodies to intermediate filament proteins in the immunohistochemical identification of human tumours: an overview. Histochem J. 1983 Jul;15(7):691–713. doi: 10.1007/BF01002988. [DOI] [PubMed] [Google Scholar]
  56. Ramaekers F. C., Verheijen R. H., Moesker O., Kant A., Vooijs G. P., Herman C. J. Mesodermal mixed tumor. Diagnosis by analysis of intermediate filament proteins. Am J Surg Pathol. 1983 Jun;7(4):381–385. [PubMed] [Google Scholar]
  57. Ramaekers F., Huysmans A., Moesker O., Kant A., Jap P., Herman C., Vooijs P. Monoclonal antibody to keratin filaments, specific for glandular epithelia and their tumors. Use in surgical pathology. Lab Invest. 1983 Sep;49(3):353–361. [PubMed] [Google Scholar]
  58. Ramaekers F., Huysmans A., Schaart G., Moesker O., Vooijs P. Tissue distribution of keratin 7 as monitored by a monoclonal antibody. Exp Cell Res. 1987 May;170(1):235–249. doi: 10.1016/0014-4827(87)90133-9. [DOI] [PubMed] [Google Scholar]
  59. Soule H. D., Vazguez J., Long A., Albert S., Brennan M. A human cell line from a pleural effusion derived from a breast carcinoma. J Natl Cancer Inst. 1973 Nov;51(5):1409–1416. doi: 10.1093/jnci/51.5.1409. [DOI] [PubMed] [Google Scholar]
  60. Southern P. J., Berg P. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J Mol Appl Genet. 1982;1(4):327–341. [PubMed] [Google Scholar]
  61. Steinert P. M., Parry D. A., Idler W. W., Johnson L. D., Steven A. C., Roop D. R. Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits. J Biol Chem. 1985 Jun 10;260(11):7142–7149. [PubMed] [Google Scholar]
  62. Steinert P. M., Roop D. R. Molecular and cellular biology of intermediate filaments. Annu Rev Biochem. 1988;57:593–625. doi: 10.1146/annurev.bi.57.070188.003113. [DOI] [PubMed] [Google Scholar]
  63. Steinert P. M., Steven A. C., Roop D. R. The molecular biology of intermediate filaments. Cell. 1985 Sep;42(2):411–420. doi: 10.1016/0092-8674(85)90098-4. [DOI] [PubMed] [Google Scholar]
  64. Steinert P. M. The dynamic phosphorylation of the human intermediate filament keratin 1 chain. J Biol Chem. 1988 Sep 15;263(26):13333–13339. [PubMed] [Google Scholar]
  65. Tokuyasu K. T., Maher P. A., Singer S. J. Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study. J Cell Biol. 1985 Apr;100(4):1157–1166. doi: 10.1083/jcb.100.4.1157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Traub P., Vorgias C. E. Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments. J Cell Sci. 1983 Sep;63:43–67. doi: 10.1242/jcs.63.1.43. [DOI] [PubMed] [Google Scholar]
  67. Vikstrom K. L., Borisy G. G., Goldman R. D. Dynamic aspects of intermediate filament networks in BHK-21 cells. Proc Natl Acad Sci U S A. 1989 Jan;86(2):549–553. doi: 10.1073/pnas.86.2.549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Wigler M., Sweet R., Sim G. K., Wold B., Pellicer A., Lacy E., Maniatis T., Silverstein S., Axel R. Transformation of mammalian cells with genes from procaryotes and eucaryotes. Cell. 1979 Apr;16(4):777–785. doi: 10.1016/0092-8674(79)90093-x. [DOI] [PubMed] [Google Scholar]
  69. van den Heuvel R. M., van Eys G. J., Ramaekers F. C., Quax W. J., Vree Egberts W. T., Schaart G., Cuypers H. T., Bloemendal H. Intermediate filament formation after transfection with modified hamster vimentin and desmin genes. J Cell Sci. 1987 Nov;88(Pt 4):475–482. doi: 10.1242/jcs.88.4.475. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES