High impact information on ADL1

• Transgenic plants harboring various deletion mutant genes of ADL1 had a yellow leaf phenotype where the cells had very few chloroplasts [1].
• Moreover, the endogenous ADL1 protein level was greatly reduced in these transgenic plants, probably due to a post-transcriptional silencing effect of the transgenes [1].
• Suborganellar fractionation studies of Arabidopsis leaf tissue revealed that a dynamin-like protein, ADL1, is localized in the thylakoid membranes of chloroplasts [1].
• A dynamin-like protein in Arabidopsis thaliana is involved in biogenesis of thylakoid membranes [1].
• We propose that ADL1-mediated membrane recycling is essential for plasma membrane formation and maintenance in plants [2].

Biological context of ADL1

• We propose that ADL1C functions in plasma membrane dynamics, and we discuss the role of the ADL1 family in plant growth and development [3].
• Members of the Arabidopsis dynamin-like gene family, ADL1, are essential for plant cytokinesis and polarized cell growth [2].
• Here, we show that two functionally redundant members of the Arabidopsis dynamin-related protein family, ADL1A and ADL1E, are essential for polar cell expansion and cell plate biogenesis. adl1A-2 adl1E-1 double mutants show defects in cell plate assembly, cell wall formation, and plasma membrane recycling [2].
• Here, we show that KN protein localisation is unaffected in keu mutant cells, which, like kn, display phragmoplast microtubules and accumulate ADL1 protein in the plane of cell division but vesicles fail to fuse with one another [4].
• Whereas the haploid gametophytes gave rise to functional gametes, the embryos behaved like single cells displaying multiple, synchronously cycling nuclei, cell cycle-dependent microtubule arrays and ADL1 accumulation between pairs of daughter nuclei [4].

Anatomical context of ADL1

• A dynamin-like protein, ADL1, is present in membranes as a high-molecular-mass complex in Arabidopsis thaliana [5].
• GFP-tagged DRP1A and DRP1C proteins were found to be associated with the cytoskeleton in G1 phase of the cell cycle [6].
• A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis [7].

Associations of ADL1 with chemical compounds

• Ca2+ increases the amount of ADL1 present in the membrane fraction, whereas cyclosporin A inhibits the membrane association [5].
• Furthermore, Ca2+ and GTP change the migration pattern of ADL1 in nondenaturing polyacrylamide gels, indicating that these chemicals influence either the complex formation and/or the conformation of the ADL1 complex [5].
• Despite the loss of ADL1Ap, the mutants did not display any defects in cytokinesis, and growth of the mutant seedlings could be rescued in tissue culture by the addition of sucrose [8].

Other interactions of ADL1

• DRP1A is responsible for vascular continuity synergistically working with VAN3 in Arabidopsis [9].
• ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery [10].

Analytical, diagnostic and therapeutic context of ADL1

• Subcellular fractionation experiments, together with gel-filtration and nondenaturing-gel electrophoresis revealed that most of ADL1 is present as a high-molecular-mass complex of 400 to 600 kD in the membrane or pellet fraction, whereas ADL1 is present in the soluble fraction as a monomer [5].
• Immunoblotting revealed that ADL1Ap expression was not detectable in the mutants [8].

References