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Abstract
Following the description of SAD1/UNC84 (SUN) domain proteins in higher plants, evidence has rapidly increased that plants contain a functional linker of nucleoskeleton and cytoskeleton (LINC) complex bridging the nuclear envelope (NE). While the SUN domain proteins appear to be highly conserved across kingdoms, other elements of the complex are not and some key components and interactions remain to be identified. This mini review examines components of the LINC complex, including proteins of the SUN domain family and recently identified plant Klarsicht/Anc/Syne-1 homology (KASH) domain proteins. First of these to be described were WIPs (WPP domain interacting proteins), which act as protein anchors in the outer NE. The plant KASH homologs are C-terminally anchored membrane proteins with the extreme C-terminus located in the nuclear periplasm; AtWIPs contain a highly conserved X-VPT motif at the C-terminus in contrast to PPPX in opisthokonts. The role of the LINC complex in organisms with a cell wall, and description of further LINC complex components will be considered, together with other potential plant-specific functions.
Highlights
The nuclear envelope (NE) fulfills many important functions: protecting and enclosing the genetic material, facilitating transport, involvement in cell signaling, and providing physical and structural bridges
This study revealed AtSUN1 and AtSUN2 to be localized to the NE in interphase and provided the first evidence of components of a putative linker of nucleoskeleton and cytoskeleton (LINC) complex in plants
Klarsicht/Anc/Syne-1 homology (KASH) DOMAIN PROTEINS; MULTI-FUNCTIONAL COMPONENTS OF THE LINC COMPLEX The term KASH domain derives from members of a family of proteins, described in D. melanogaster (Klarsicht), C elegans, (ANC-1; Starr and Han, 2002) and mammals (Syne-1 and 2, known as Nesprin 1 and 2; Apel et al, 2000) which interact with SUN domain proteins (Starr and Fridolfsson, 2010)
Summary
The nuclear envelope (NE) fulfills many important functions: protecting and enclosing the genetic material, facilitating transport, involvement in cell signaling, and providing physical and structural bridges. These protein bridges have multiple functions, providing support and anchorage for the genetic material and nucleoskeleton, positioning, and moving the nucleus and acting as a pathway of signaling. While these functions and structures are conserved in eukaryotes, there are marked differences in the proteins that are involved (see below and Zhou and Meier, 2013). The major bridge in this space is the linker of nucleoskeleton and cytoskeleton (LINC) complex (Crisp et al, 2006) It is conserved across eukaryotes and has remarkable diversity of function through modification of two families of constituent proteins. A coiled coil domain is located between the transmembrane domain and the SUN domain in the nuclear www.frontiersin.org
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