The fates of chicken nuclear lamin proteins during mitosis: evidence for a reversible redistribution of lamin B2 between inner nuclear membrane and elements of the endoplasmic reticulum

doi:10.1083/jcb.107.2.397

This Article

	Full Text (PDF, 5300K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Stick, R.
	Articles by Nigg, E. A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Stick, R.
	Articles by Nigg, E. A.

Social Bookmarking

	What's this?

ARTICLES

The fates of chicken nuclear lamin proteins during mitosis: evidence for a reversible redistribution of lamin B2 between inner nuclear membrane and elements of the endoplasmic reticulum

R Stick, B Angres, CF Lehner and EA Nigg
Max-Planck-Institut fur Entwicklungsbiologie, Abt. fur Zellbiologie, Tubingen, Federal Republic of Germany.

In chicken, three structurally distinct nuclear lamin proteins have been described. According to their migration on two-dimensional gels, these proteins have been designated as lamins A, B1, and B2. To investigate the functional relationship between chicken lamins and their mammalian counterparts, we have examined here the state of individual chicken lamin proteins during mitosis. Current models proposing functional specializations of mammalian lamin subtypes are in fact largely based on the observation that during mitosis mammalian lamin B remains associated with membrane vesicles, whereas lamins A and C become freely soluble. Cell fractionation experiments combined with immunoblotting show that during mitosis both chicken lamins B1 and B2 remain associated with membranes, whereas lamin A exists in a soluble form. In situ immunoelectron microscopy carried out on mitotic cells also reveals membrane association of lamin B2, whereas the distribution of lamin A is random. From these results we conclude that both chicken lamins B1 and B2 may functionally resemble mammalian lamin B. Interestingly, immunolabeling of mitotic cells revealed an association of lamin B2 with extended membrane cisternae that resembled elements of the endoplasmic reticulum. Quantitatively, we found that all large endoplasmic reticulum-like membranes present in metaphase cells were decorated with lamin B2-specific antibodies. Given that labeling of these mitotic membranes was lower than labeling of interphase nuclear envelopes, it appears likely that during mitotic disassembly and reassembly of the nuclear envelope lamin B2 may reversibly distribute between the inner nuclear membrane and the endoplasmic reticulum.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Senda, T., Iizuka-Kogo, A., Shimomura, A. (2005). Visualization of the Nuclear Lamina in Mouse Anterior Pituitary Cells and Immunocytochemical Detection of Lamin A/C by Quick-freeze Freeze-substitution Electron Microscopy. J. Histochem. Cytochem. 53: 497-507 [Abstract] [Full Text]
Daigle, N., Beaudouin, J., Hartnell, L., Imreh, G., Hallberg, E., Lippincott-Schwartz, J., Ellenberg, J. (2001). Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. JCB 154: 71-84 [Abstract] [Full Text]
Hofemeister, H., Weber, K., Stick, R. (2000). Association of Prenylated Proteins with the Plasma Membrane and the Inner Nuclear Membrane Is Mediated by the Same Membrane-targeting Motifs. Mol. Biol. Cell 11: 3233-3246 [Abstract] [Full Text]
Lourim, D, Krohne, G (1999). Chromatin binding and polymerization of the endogenous Xenopus egg lamins: the opposing effects of glycogen and ATP. J. Cell Sci. 111: 3675-3686 [Abstract]
Drummond, S., Ferrigno, P., Lyon, C., Murphy, J., Goldberg, M., Allen, T., Smythe, C., Hutchison, C. J. (1999). Temporal Differences in the Appearance of NEP-B78 and an LBR-like Protein during Xenopus Nuclear Envelope Reassembly Reflect the Ordered Recruitment of Functionally Discrete Vesicle Types. JCB 144: 225-240 [Abstract] [Full Text]
Duband-Goulet, I, Courvalin, J., Buendia, B (1998). LBR, a chromatin and lamin binding protein from the inner nuclear membrane, is proteolyzed at late stages of apoptosis. J. Cell Sci. 111: 1441-1451 [Abstract]
Ellenberg, J., Siggia, E. D., Moreira, J. E., Smith, C. L., Presley, J. F., Worman, H. J., Lippincott-Schwartz, J. (1997). Nuclear Membrane Dynamics and Reassembly in Living Cells: Targeting of an Inner Nuclear Membrane Protein in Interphase and Mitosis. JCB 138: 1193-1206 [Abstract] [Full Text]
Pugh, G., Coates, P., Lane, E., Raymond, Y, Quinlan, R. (1997). Distinct nuclear assembly pathways for lamins A and C lead to their increase during quiescence in Swiss 3T3 cells. J. Cell Sci. 110: 2483-2493 [Abstract]
Ellis, D., Jenkins, H, Whitfield, W., Hutchison, C. (1997). GST-lamin fusion proteins act as dominant negative mutants in Xenopus egg extract and reveal the function of the lamina in DNA replication. J. Cell Sci. 110: 2507-2518 [Abstract]
Klapper, M, Exner, K, Kempf, A, Gehrig, C, Stuurman, N, Fisher, P., Krohne, G (1997). Assembly of A- and B-type lamins studied in vivo with the baculovirus system. J. Cell Sci. 110: 2519-2532 [Abstract]
Wiese, C, Goldberg, M., Allen, T., Wilson, K. (1997). Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent 'envelope smoothing' event. J. Cell Sci. 110: 1489-1502 [Abstract]
Paddy, M. R., Saumweber, H., Agard, D. A., Sedat, J. W. (1996). Time-resolved, in vivo studies of mitotic spindle formation and nuclear lamina breakdown in Drosophila early embryos. J. Cell Sci. 109: 591-607 [Abstract]
Zhang, C, Jenkins, H, Goldberg, M., Allen, T., Hutchison, C. (1996). Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract. J. Cell Sci. 109: 2275-2286 [Abstract]
Goldberg, M, Jenkins, H, Allen, T, Whitfield, W., Hutchison, C. (1995). Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: evidence from cell-free egg extracts. J. Cell Sci. 108: 3451-3461 [Abstract]
Riemer, D, Stuurman, N, Berrios, M, Hunter, C, Fisher, P., Weber, K (1995). Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins. J. Cell Sci. 108: 3189-3198 [Abstract]
Hutchison, C., Bridger, J., Cox, L., Kill, I. (1994). Weaving a pattern from disparate threads: lamin function in nuclear assembly and DNA replication. J. Cell Sci. 107: 3259-3269 [Abstract]
Hennekes, H, Nigg, E. (1994). The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J. Cell Sci. 107: 1019-1029 [Abstract]
Goldberg, M., Allen, T. (1993). The nuclear pore complex: three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis. J. Cell Sci. 106: 261-274 [Abstract]
Jenkins, H, Holman, T, Lyon, C, Lane, B, Stick, R, Hutchison, C (1993). Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix. J. Cell Sci. 106: 275-285 [Abstract]
Minguez, A, Moreno Diaz de la Espina, S (1993). Immunological characterization of lamins in the nuclear matrix of onion cells. J. Cell Sci. 106: 431-439 [Abstract]