Related Experiment Video
Updated: May 6, 2026

Author Spotlight: Microscopic Analysis of Protein Localization at Plasmodesmata in Plants
Published on: November 1, 2024
NMCP/LINC proteins: putative lamin analogs in plants?
Malgorzata Ciska1, Susana Moreno Diaz de la Espina1
1Department of Cell and Molecular Biology; Biological Research Centre; CSIC; Madrid, Spain.
Abstract:
Lamins are the main components of the metazoan lamina, and while the organization of the nuclear lamina of metazoans and plants is similar, there are apparently no genes encoding lamins or most lamin-binding proteins in plants. Thus, the plant lamina is not lamin-based and the proteins that form this structure are still to be characterized. Members of the plant NMCP/LINC/CRWN protein family share the typical tripartite structure of lamins, although the 2 exhibit no sequence similarity. However, given the many similarities between NMCP/LINC/CRWN proteins and lamins (structural organization, position of conserved regions, sub-nuclear distribution, solubility, and pattern of expression), these proteins are good candidates to carry out the functions of lamins in plants. Moreover, functional analysis of NMCP/LINC mutants has revealed their involvement in maintaining nuclear size and shape, another activity fulfilled by lamins. This review summarizes the current understanding of NMCP/LINC proteins and discusses future studies that will be required to demonstrate definitively that these proteins are plant analogs of lamins.
More Related Videos
Related Concept Videos
Protein Transport to the Inner Chloroplast Membrane
Cell Signaling in Plants
lncRNA - Long Non-coding RNAs
Laminins are the Adhesive Proteins of Basal Lamina
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
Protein Transport to the Thylakoids
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.

