The lamin CxxM motif promotes nuclear membrane growth

Prüfert, Kristina; Vogel, Annette; Krohne, Georg

doi:10.1242/jcs.01532

Cited by 103 publications

(96 citation statements)

References 58 publications

(42 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Exogenous expression of lipidated nuclear proteins induces the formation of intranuclear membrane-like arrays. [26][27][28] To characterize the nature of these arrays FLAG-tagged lamin B2 was expressed in Xenopus oocytes by nuclear injection of plasmid DNA. NE spreads were analyzed by immunofluorescence microscopy ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Intranuclear membrane-like arrays are also induced by overexpressing intranuclear proteins with a lipidation motif, as seen for lamins overexpressed in amphibian oocytes 26 or other cell types. 27,28 Induction of the arrays strictly depends on the presence of either an isoprenylation or a myristoylation motif. Nuclear translocation of lamins is mediated by binding to importin α/β via a classical NLS 29 followed by uptake through the central pore of the NPC.…”

Section: Resultsmentioning

confidence: 99%

“…The intranuclear membrane arrays described here are attached to the INM but continuity between these membranes and the INM has never been observed. 26,28 We therefore analyzed whether the intranuclear membrane arrays are part of the endomembrane system or might be formed de novo by a hitherto unknown mechanism. If derived from the NE/ER membranes it is reasonable to assume that the intranuclear membranes will contain typical ER proteins, be it luminal or integral membrane proteins.…”

Section: Resultsmentioning

confidence: 99%

“…Lamin-induced intranuclear membrane formation is dependent on lipid modification, either by farnesylation 26,28 or by myristoylation. 27 We have previously shown that an NLS in conjunction with a CaaX motif can act as minimal targeting motif for the association of proteins with the INM 39 and that expression of these proteins induces intranuclear vesicular and tubular structures.…”

Section: Resultsmentioning

confidence: 99%

See 3 more Smart Citations

Intranuclear membranes induced by lipidated proteins are derived from the nuclear envelope

Linde¹,

Stick²

2010

Nucleus

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Intranuclear membranes induced by lipidated proteins are derived from the nuclear envelope

Linde¹,

Stick²

2010

Nucleus

View full text Add to dashboard Cite

“…In contrast, LAP2␣ shares only the N-terminal 187 amino acids with the other isoforms, including the LEM and LEM-like domains, but otherwise possesses a unique 506-amino-acid C-terminal region without a transmembrane domain (see Fig. 1A), encoded by one large exon found only in mammals (10).…”

mentioning

confidence: 99%

Lamina-associated Polypeptide 2-α Forms Homo-trimers via Its C Terminus, and Oligomerization Is Unaffected by a Disease-causing Mutation

Snyers

Vlcek

Dechat

et al. 2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

The nucleoplasmic protein, Lamina-associated polypeptide (LAP) 2␣, is one of six alternatively spliced products of the LAP2gene, which share a common N-terminal region. In contrast to the other isoforms, which also share most of their C termini, LAP2␣ has a large unique C-terminal region that contains binding sites for chromatin, A-type lamins, and retinoblastoma protein. By immunoprecipitation analyses of LAP2␣ complexes from cells expressing differently tagged LAP2␣ proteins and fragments, we demonstrate that LAP2␣ forms higher order structures containing multiple LAP2␣ molecules in vivo and that complex formation is mediated by the C terminus. Solid phase binding assays using recombinant and in vitro translated LAP2␣ fragments showed direct interactions of LAP2␣ C termini. Cross-linking of LAP2␣ complexes and multiangle light scattering of purified LAP2␣ revealed the existence of stable homo-trimers in vivo and in vitro. Finally, we show that, in contrast to the LAP2␣-lamin A interaction, its self-association is not affected by a disease-linked single point mutation in the LAP2␣ C terminus.The nuclear envelope comprises the inner and outer nuclear membranes, the nuclear pore complexes, and the nuclear lamina, which underlies the inner nuclear membrane (1, 2). The nuclear lamina is the major structural framework in the nucleus of multicellular eukaryotes and is composed of a filamentous meshwork of type V intermediate filament proteins, the lamins. B-type lamins, encoded by two human genes (LMNB1 and LMNB2), are essential for cell viability. In contrast, the four A-type lamins (A, C, C2, and A⌬10), representing splicing isoforms of the LMNA gene, are dispensable for viability of individual cells but have crucial functions in tissue organization after birth (3, 4).In addition to the lamins, the nuclear lamina contains a number of integral membrane proteins of the inner nuclear membrane, the best characterized of which are the Lamin B receptor, Lamina-associated polypeptide (LAP), 4 and the three LEM domain-containing proteins LAP2␤, emerin and MAN1 (5, 6). All these proteins interact with lamin A/C and/or B and contribute to anchorage of the nuclear membrane to the lamina. The LEM domain, a conserved 40-amino-acid motif located near the N terminus of the LEM family proteins, interacts with the DNA-binding protein barrier-to-autointegration factor (BAF) and mediates the binding of these proteins to chromatin (7). In LAP2 proteins, a LEM-like segment at the very N terminus has been shown to interact with DNA directly (8).The family of LAP2 proteins includes six alternatively spliced isoforms derived from the same gene (9). Most LAP2 isoforms are closely related structurally and functionally and are localized to the inner nuclear membrane, such as LAP2␤. In contrast, LAP2␣ shares only the N-terminal 187 amino acids with the other isoforms, including the LEM and LEM-like domains, but otherwise possesses a unique 506-amino-acid C-terminal region without a transmembrane domain (see Fig. 1A), encoded by one large exon...

show abstract

Towards an integrated understanding of the structure and mechanics of the cell nucleus

et al. 2008

View full text Add to dashboard Cite

Changes in the shape and structural organization of the cell nucleus occur during many fundamental processes including development, differentiation and aging. In many of these processes, the cell responds to physical forces by altering gene expression within the nucleus. How the nucleus itself senses and responds to such mechanical cues is not well understood. In addition to these external forces, epigenetic modifications of chromatin structure inside the nucleus could also alter its physical properties. To achieve a better understanding, we need to elucidate the relationship between nuclear structure and material properties. Recently, new approaches have been developed to systematically investigate nuclear mechanical properties. These experiments provide important new insights into the disease mechanism of a growing class of tissue-specific disorders termed 'nuclear envelopathies'. Here we review our current understanding of what determines the shape and mechanical properties of the cell nucleus.

show abstract

The lamin CxxM motif promotes nuclear membrane growth

Cited by 103 publications

References 58 publications

Intranuclear membranes induced by lipidated proteins are derived from the nuclear envelope

Intranuclear membranes induced by lipidated proteins are derived from the nuclear envelope

Lamina-associated Polypeptide 2-α Forms Homo-trimers via Its C Terminus, and Oligomerization Is Unaffected by a Disease-causing Mutation

Towards an integrated understanding of the structure and mechanics of the cell nucleus

Contact Info

Product

Resources

About