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.

Stick, Reimer; Angres, Brigitte; Lehner, Christian F.; Nigg, Erich A.

doi:10.1083/jcb.107.2.397

Cited by 104 publications

(52 citation statements)

References 38 publications

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“…On the other hand, the'NE membrane shares biochemical markers with the ER and is often continuous with it (Franke, 1974). Since lamin B also remains associated with the ER during mitosis in chick tissue culture cells (Stick et al, 1988), one would expect NE membrane proteins to copurify with ER proteins. However, we find relatively little ot-glucosidase activity in NEP-B, suggesting that at least some membrane proteins of the NE do not segregate with the ER vesicles.…”

Section: Discussionmentioning

confidence: 99%

A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs.

Vigers

Lohka

1991

The Journal of Cell Biology

148

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Abstract. Extracts from Xenopus eggs capable of nuclear envelope assembly in vitro were fractionated by differential and density gradient centrifugation. Nuclear envelope assembly was found to require soluble components in the cytosol and two distinct particulate fractions, which we have called nuclear envelope precursor fractions A and B (NEP-A and NEP-B). Both NEP-A and NEP-B are sensitive to treatments with trypsin, sodium carbonate, and detergents, but can be distinguished from each other by their sensitivities to high salt and N-ethylmaleimide and by their levels of o~-glucosidase activity. Vesicles in NEP-B bind to chromatin, whereas those in NEP-A do not. NEP-B may therefore be involved in the targeting of membranes to the surface of the chromatin, whereas NEP-A may provide a pool of vesicles that contributes many of the nuclear envelope membranes. NEP-B may also play a role in the assembly of nuclear pore complexes because the density of nuclear pores in the resuiting envelope is dependent on the ratio of NEP-B to NEP-A in the reconstituted extract.

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Section: Discussionmentioning

confidence: 99%

A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs.

Vigers

Lohka

1991

The Journal of Cell Biology

148

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“…B-type lamins of mammals and birds are associated with mitotic NE-derived membranes (Gerace and Blobel, 1980;Stick et al, 1988;Meier and Georgatos, 1994). The cDNA sequences of the two avian and several mammalian B-type lamins indicate that all of these proteins carry a CaaX motif, but none contains additional membrane-targeting signals such as a basic cluster or an extra cysteine residue.…”

Section: Discussionmentioning

confidence: 99%

“…A-type lamins, which lose their isoprene moiety soon after incorporation into the lamina, become freely soluble upon mitotic nuclear envelope (NE) breakdown (Weber et al, 1989;Beck et al, 1990;Kilic et al, 1999). Somatic B-type lamins, in contrast, are permanently isoprenylated and, although depolymerized during mitosis, remain asso-ciated with remnants of NE membranes (Gerace and Blobel, 1980;Stick et al, 1988;Nigg et al, 1992;Hennekes and Nigg, 1994). However, as shown by studies of amphibian egg maturation, the CaaX-dependent modifications are not sufficient to mediate the stable membrane association of lamins.…”

Section: Introductionmentioning

confidence: 99%

“…E-mail address: r.stick@dkfz.de. Abbreviations used: GFP, Green Fluorescent Protein; NE, nuclear envelope; NLS, nuclear localization signal; pcCMT, prenylcysteine carboxyl methyltransferase; PM, plasma membrane.© 2000 by The American Society for Cell Biology 3233 ciated with remnants of NE membranes (Gerace and Blobel, 1980;Stick et al, 1988;Nigg et al, 1992;Hennekes and Nigg, 1994). However, as shown by studies of amphibian egg maturation, the CaaX-dependent modifications are not sufficient to mediate the stable membrane association of lamins.…”

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confidence: 99%

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Association of Prenylated Proteins with the Plasma Membrane and the Inner Nuclear Membrane Is Mediated by the Same Membrane-targeting Motifs

Hofemeister

Weber

Stick

2000

MBoC

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Targeting of nuclear lamins to the inner nuclear envelope membrane requires a nuclear localization signal and CaaX motif-dependent posttranslational modifications, including isoprenylation and carboxyl methylation. These modifications, although necessary for membrane targeting, are not sufficient to mediate stable association with membranes. We show that two variants of lamin B3 (i.e., B3a and B3b) exist in Xenopus oocytes. They are encoded by two alternatively spliced, developmentally regulated mRNAs. The two lamin variants differ greatly in their membrane association in meiotically matured eggs. The presence of an extra cysteine residue (as a potential palmitoylation site) and a basic cluster in conjunction with the CaaX motif function as secondary targeting signals responsible for the stable membrane association of lamin B3b in Xenopus eggs. Moreover, transfection experiments with Green Fluorescent Protein lamin tail chimeras and with a Green Fluorescent Protein N-Ras chimera show that these secondary motifs are sufficient to target proteins to the inner nuclear membrane and/or the plasma membrane. Implications for the intracellular trafficking of doubly lipidated proteins are discussed. INTRODUCTIONMembrane targeting of certain eukaryotic proteins depends on posttranslational lipidation. A major class of these proteins contains CaaX motifs at their COOH termini. The CaaX motif is the target of a series of posttranslational modifications, including isoprenylation, proteolytic trimming, and carboxyl methylation. In a first step, a farnesyl or geranylgeranyl lipid is added via a stable thioether linkage to the CaaX cysteine (Glomset and Farnsworth, 1994;Zhang and Casey, 1996). The substrate specificity for farnesyltransferase versus geranylgeranyltransferase is determined by the residue in the X position of the CaaX motif (Casey and Seabra, 1996). Next, a specific protease cleaves the aaX residues from the prenylated protein. Finally, the terminal prenylcysteine is recognized by a prenylcysteine carboxyl methyltransferase (pcCMT) that methylesterifies the carboxyl group. Thus, a hydrophobic COOH-terminal region is generated in an otherwise hydrophilic molecule. Proteins that contain a CaaX motif include the Ras proteins and many other small G proteins, the heterotrimeric large G proteins, fungal mating pheromones, and most nuclear lamins (Glomset and Farnsworth, 1994;Reuther and Der, 2000). Prenylated proteins exert a variety of different functions. For many of these proteins, the importance of prenylation for their function has been shown (Loewinger and McKeon, 1988;Hancock et al., 1989Hancock et al., , 1991aHoltz et al., 1989;Krohne et al., 1989;Kitten and Nigg, 1991;Nigg et al., 1992;Hennekes and Nigg, 1994). Large G proteins are geranylgeranylated, whereas Ras proteins, the fungal mating pheromones, and lamins are farnesylated (Moores et al., 1991;Zhang and Casey, 1996). Proteins carrying the same CaaX-dependent modifications are located in different membrane compartments, indicating that additional factors...

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“…The mAb 9E10 (ATCC CRL 1729) specifically recognizes an epitope in the decapeptide EQKLISEEDL of the human c-myc protein (Evan et al, 1985), and mAb L3-4B4 (kindly provided by Dr. R. Stick, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany) reacts with -chicken and mammalian lamin A, but not with Xenopus lamins (Lehner et al, 1987;Stick et al, 1988). In one set of experiments, mAb b7-1A9-M9 directed against the histone-binding protein nucleoplasmin from Xenopus …”

Section: Materials and Methods Antibodiesmentioning

confidence: 99%

Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.

Zirwes

Kouzmenko

Peters

et al. 1997

MBoC

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To identify the element(s) in nucleolar proteins which determine nucleolus-specific topogenesis, we have used different kinds of cDNA constructs encoding various chimeric combinations of mutants of the constitutive nucleolar protein N038 (B23): 1) with an amino terminally placed short "myc tag"; 2) with two different carboxyl terminally attached large a-helical coiled coil structures, the lamin A rod domain or the rod domain of vimentin; 3) with the sequence-related nucleoplasmic histone-binding protein nucleoplasmin; and 4) with the soluble cytoplasmic protein pyruvate kinase. To avoid the problem of formation of complexes with endogenous wild-type (wt) molecules and "piggyback" localization, special care was taken to secure that the mutants and chimeras used did not oligomerize as is typical of protein N038 (B23). Using microinjection and transfection of cultured cells, we found that the segment comprising the amino-terminal 123 amino acids (aa) alone was sufficient to effect nucleolar accumulation of the construct molecules, including the chimeras with the entire rod domains of lamin A and vimentin. However, when the amino-terminal 109 aa were deleted, the molecules still associated with the nucleolus. The results of further deletion experiments and of domain swaps with nucleoplasmin all point to the topogenic importance of two independent molecular regions located at both the amino-and carboxyl-terminal end. Our definition of dominant elements determining the nucleolar localization of protein N038 (B23) as well as of diverse nonnucleolar proteins will help to identify its local binding partner(s) and functions, the construction of probes examining other proteins or sequence elements within the nucleolar microenvironment, and the generation of cells with an altered nuclear architecture.

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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.

Cited by 104 publications

References 38 publications

A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs.

A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs.

Association of Prenylated Proteins with the Plasma Membrane and the Inner Nuclear Membrane Is Mediated by the Same Membrane-targeting Motifs

Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.

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