MUR3 (MURUS3), also known as KATAMARI1 (KAM1), is a plant-specific Golgi membrane protein critical for actin filament organization and cell wall biosynthesis. It interacts with actin to regulate Golgi-mediated cytoskeletal dynamics, impacting cell structure and intracellular trafficking .
Antibodies against MUR3 were generated using specific epitopes for immunoprecipitation and localization studies. Key details include:
MUR3 antibodies confirmed the protein’s exclusive localization on Golgi membranes using fluorescence-tagged constructs in Arabidopsis protoplasts .
Truncated MUR3 (N-terminal 120 amino acids) retained Golgi targeting, indicating this region is sufficient for localization .
Immunoprecipitation assays demonstrated direct binding between MUR3 and actin filaments (Figure 8C in ).
This interaction suggests MUR3 links Golgi function to actin dynamics, enabling vesicle trafficking and cell wall synthesis .
Mutant Arabidopsis lines lacking MUR3 exhibited disrupted actin networks, validating its role in cytoskeletal organization .
MUR3 antibodies were critical in identifying its regulatory role in Golgi-mediated secretion pathways .
MUR3 antibodies have been used to:
Map subcellular localization via immunofluorescence (e.g., merged signals with GFP-Golgi markers) .
Study protein-protein interactions through co-immunoprecipitation (e.g., actin-MUR3 complexes) .
Validate gene-editing outcomes in plant cell biology (e.g., CRISPR mutants) .
Current MUR3 antibodies exhibit cross-reactivity in human cells (e.g., HeLa), raising questions about evolutionary conservation .
No commercial monoclonal antibodies are yet available; existing tools are polyclonal, limiting reproducibility .
Future studies could explore MUR3’s role in human diseases involving Golgi dysfunction (e.g., neurodegenerative disorders).