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Evolution: functional evolution of nuclear structure.

Wilson KL, Dawson SC - J. Cell Biol. (2011)

Bottom Line: Recent studies have identified many components of the nuclear envelope in living Opisthokonts, the eukaryotic supergroup that includes fungi and metazoan animals.These components include diverse chromatin-binding membrane proteins, and membrane proteins with adhesive lumenal domains that may have contributed to the evolution of nuclear membrane architecture.Further discoveries about the nucleoskeleton suggest that the evolution of nuclear structure was tightly coupled to genome partitioning during mitosis.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. klwilson@jhmi.edu

ABSTRACT
The evolution of the nucleus, the defining feature of eukaryotic cells, was long shrouded in speculation and mystery. There is now strong evidence that nuclear pore complexes (NPCs) and nuclear membranes coevolved with the endomembrane system, and that the last eukaryotic common ancestor (LECA) had fully functional NPCs. Recent studies have identified many components of the nuclear envelope in living Opisthokonts, the eukaryotic supergroup that includes fungi and metazoan animals. These components include diverse chromatin-binding membrane proteins, and membrane proteins with adhesive lumenal domains that may have contributed to the evolution of nuclear membrane architecture. Further discoveries about the nucleoskeleton suggest that the evolution of nuclear structure was tightly coupled to genome partitioning during mitosis.

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Proposed contributions of membrane proteins to the evolution of nuclear structure. Different types of proteins are proposed to have contributed to the incremental evolution of nuclear structure including soluble proto-coatomer proteins (aqua), DNA- or chromatin-binding membrane proteins (navy blue), centromere- or par system–associated membrane proteins (light purple), homotypic membrane “adhesion” proteins (yellow), and heterotypic membrane adhesion proteins (teal and light green). Blue indicates partitioning proteins (actin, ATPase, DNA-binding coiled-coil protein, tubulin), many of which are components of the nucleoskeleton in living Opisthokonts (see text).
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fig2: Proposed contributions of membrane proteins to the evolution of nuclear structure. Different types of proteins are proposed to have contributed to the incremental evolution of nuclear structure including soluble proto-coatomer proteins (aqua), DNA- or chromatin-binding membrane proteins (navy blue), centromere- or par system–associated membrane proteins (light purple), homotypic membrane “adhesion” proteins (yellow), and heterotypic membrane adhesion proteins (teal and light green). Blue indicates partitioning proteins (actin, ATPase, DNA-binding coiled-coil protein, tubulin), many of which are components of the nucleoskeleton in living Opisthokonts (see text).

Mentions: Two decades of intensive investigation have yielded a wealth of information about the NPC including its ∼30 constituent proteins (nucleoporins) and their stoichiometry, biochemistry, assembly, and three-dimensional positions within the NPC (Doucet and Hetzer, 2010; Fichtman et al., 2010; Wente and Rout, 2010). This knowledge includes the functions of specific folded domains within each nucleoporin (Devos et al., 2006). Remarkably, the components and structure of one NPC subcomplex (vertebrate Nup107-160 complex) resemble the membrane-bending protein coats that generate vesicles in the secretory and endomembrane pathways (Fig. 2; Devos et al., 2004). This stunning finding led to the proto-coatomer hypothesis, which suggests that both structures evolved from an ancestral membrane-curving protein(s) (Fig. 2; Devos et al., 2004; Hsia et al., 2007; Debler et al., 2008; Leksa and Schwartz, 2010).


Evolution: functional evolution of nuclear structure.

Wilson KL, Dawson SC - J. Cell Biol. (2011)

Proposed contributions of membrane proteins to the evolution of nuclear structure. Different types of proteins are proposed to have contributed to the incremental evolution of nuclear structure including soluble proto-coatomer proteins (aqua), DNA- or chromatin-binding membrane proteins (navy blue), centromere- or par system–associated membrane proteins (light purple), homotypic membrane “adhesion” proteins (yellow), and heterotypic membrane adhesion proteins (teal and light green). Blue indicates partitioning proteins (actin, ATPase, DNA-binding coiled-coil protein, tubulin), many of which are components of the nucleoskeleton in living Opisthokonts (see text).
© Copyright Policy - openaccess
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3198171&req=5

fig2: Proposed contributions of membrane proteins to the evolution of nuclear structure. Different types of proteins are proposed to have contributed to the incremental evolution of nuclear structure including soluble proto-coatomer proteins (aqua), DNA- or chromatin-binding membrane proteins (navy blue), centromere- or par system–associated membrane proteins (light purple), homotypic membrane “adhesion” proteins (yellow), and heterotypic membrane adhesion proteins (teal and light green). Blue indicates partitioning proteins (actin, ATPase, DNA-binding coiled-coil protein, tubulin), many of which are components of the nucleoskeleton in living Opisthokonts (see text).
Mentions: Two decades of intensive investigation have yielded a wealth of information about the NPC including its ∼30 constituent proteins (nucleoporins) and their stoichiometry, biochemistry, assembly, and three-dimensional positions within the NPC (Doucet and Hetzer, 2010; Fichtman et al., 2010; Wente and Rout, 2010). This knowledge includes the functions of specific folded domains within each nucleoporin (Devos et al., 2006). Remarkably, the components and structure of one NPC subcomplex (vertebrate Nup107-160 complex) resemble the membrane-bending protein coats that generate vesicles in the secretory and endomembrane pathways (Fig. 2; Devos et al., 2004). This stunning finding led to the proto-coatomer hypothesis, which suggests that both structures evolved from an ancestral membrane-curving protein(s) (Fig. 2; Devos et al., 2004; Hsia et al., 2007; Debler et al., 2008; Leksa and Schwartz, 2010).

Bottom Line: Recent studies have identified many components of the nuclear envelope in living Opisthokonts, the eukaryotic supergroup that includes fungi and metazoan animals.These components include diverse chromatin-binding membrane proteins, and membrane proteins with adhesive lumenal domains that may have contributed to the evolution of nuclear membrane architecture.Further discoveries about the nucleoskeleton suggest that the evolution of nuclear structure was tightly coupled to genome partitioning during mitosis.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. klwilson@jhmi.edu

ABSTRACT
The evolution of the nucleus, the defining feature of eukaryotic cells, was long shrouded in speculation and mystery. There is now strong evidence that nuclear pore complexes (NPCs) and nuclear membranes coevolved with the endomembrane system, and that the last eukaryotic common ancestor (LECA) had fully functional NPCs. Recent studies have identified many components of the nuclear envelope in living Opisthokonts, the eukaryotic supergroup that includes fungi and metazoan animals. These components include diverse chromatin-binding membrane proteins, and membrane proteins with adhesive lumenal domains that may have contributed to the evolution of nuclear membrane architecture. Further discoveries about the nucleoskeleton suggest that the evolution of nuclear structure was tightly coupled to genome partitioning during mitosis.

Show MeSH
Related in: MedlinePlus