Unknown

Dataset Information

0

A malectin domain kinesin functions in pollen and seed development in Arabidopsis.


ABSTRACT: The kinesin family is greatly expanded in plants compared with animals and, with more than a third up-regulated in expression during cell division, it has been suggested that this expansion facilitated complex plant-specific cytoskeletal rearrangements. The cell cycle-regulated kinesins include two with an N-terminal malectin domain, a protein domain that has been shown to bind polysaccharides and peptides when found extracellularly in receptor-like kinases. Although malectin domain kinesins are evolutionarily deep rooted, their function in plants remains unclear. Here we show that loss of MALECTIN DOMAIN KINESIN 2 (MDKIN2) results in stochastic developmental defects in pollen, embryo, and endosperm. High rates of seed abnormalities and abortion occur in mdkin2 mutants through a partial maternal effect. No additive effect or additional developmental defects were noted in mdkin1 mdkin2 double mutants. MDKIN2 is expressed in regions of cell division throughout the plant. Subcellular localization of MDKIN2 indicates a role in cell division, with a possible secondary function in the nuclei. Our results reveal a non-essential but important role for a malectin domain kinesin during development in plants.

SUBMITTER: Galindo-Trigo S 

PROVIDER: S-EPMC7094084 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

A malectin domain kinesin functions in pollen and seed development in Arabidopsis.

Galindo-Trigo Sergio S   Grand Thomas M TM   Voigt Christian A CA   Smith Lisa M LM  

Journal of experimental botany 20200301 6


The kinesin family is greatly expanded in plants compared with animals and, with more than a third up-regulated in expression during cell division, it has been suggested that this expansion facilitated complex plant-specific cytoskeletal rearrangements. The cell cycle-regulated kinesins include two with an N-terminal malectin domain, a protein domain that has been shown to bind polysaccharides and peptides when found extracellularly in receptor-like kinases. Although malectin domain kinesins are  ...[more]

Similar Datasets

| S-EPMC1559784 | biostudies-literature
| S-EPMC4201294 | biostudies-literature
| S-EPMC6468697 | biostudies-literature
| S-EPMC8287233 | biostudies-literature
| S-EPMC3040128 | biostudies-literature
| S-EPMC3695568 | biostudies-literature
| S-EPMC7783096 | biostudies-literature
| S-EPMC3287576 | biostudies-literature
| S-EPMC7876099 | biostudies-literature
| S-EPMC8353282 | biostudies-literature