Abstract
The functional organization of the nuclear envelope (NE) is only just emerging in plants with the recent characterization of NE protein complexes and their molecular links to the actin cytoskeleton. The NE also plays a role in microtubule nucleation by recruiting γ-Tubulin Complexes (γ-TuCs) which contribute to the establishment of a robust mitotic spindle. γ-tubulin Complex Protein 3 (GCP3)-interacting proteins (GIPs) have been identified recently as integral components of γ-TuCs. GIPs have been conserved throughout evolution and are also named MZT1 (mitotic-spindle organizing protein 1). This review focuses on recent data investigating the role of GIP/MZT1 at the NE, including insights from the study of GIP partners. It also uncovers new functions for GIP/MZT1 during interphase and highlights a current view of NE-associated components which are critical for nuclear shaping during both cell division and differentiation.
Highlights
The nuclear envelope (NE) primarily appeared as a selective barrier between the nucleoplasm and the cytoplasm of Eukaryote cells
Bridging the inner (INM) and the outer (ONM) nuclear membranes, LInker of the Nucleoskeleton and the Cytoskeleton (LINC) complexes are considered as force transducers between the nuclear lamina and the cytoskeleton (Wang et al, 2012)
ROLE OF GCP3 Interacting Proteins (GIPs) AT THE ONM in γ-Tubulin Complexes (γ-TuCs) RECRUITMENT AND ANCHORING In plants, the whole nuclear surface has been characterized as a MT nucleating site (Erhardt et al, 2002; Seltzer et al, 2003; Canaday et al, 2005; Seltzer et al, 2007); perinuclear MT arrays may connect the NE to the cellular periphery and participate in signal transduction
Summary
The nuclear envelope (NE) primarily appeared as a selective barrier between the nucleoplasm and the cytoplasm of Eukaryote cells. The recent discovery of GIP proteins (Janski et al, 2008, 2012, Nakamura et al, 2012) as integral components of the γ-TuC and the GIP’s partnership (Batzenschlager et al, 2013) tend to ascribe GIP a major role in NE shaping in both cycling and differentiated cells.
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