Unraveling the Role of Patellin1 in Expansive and Polarized Cell Growth
Conference Year
2024
Abstract
The Patellin gene family, a subgroup of Sec14-like proteins containing lipid binding domains, has been shown to play a role in membrane trafficking in Arabidopsis. The family members PATL3 and PATL6 have been implicated in impeding viral movement by binding to viral movement proteins (Peiro et al., 2014) . In addition, the patl2 patl4 patl5 patl6 quadruplet mutant, is defective in recycling of the auxin transport proteins PIN1 and PIN2 (Tejos et al., 2018). PATL1 localizes to the cell plate and the plasma membrane, and this is thought to be facilitated through its affinity for specific species of phosphoinositides (Peterman et al., 2004). We have characterized PATL1's involvement in expansive and polarized growth by examining two T-DNA null alleles (patl1-2 and patl1-3) in Arabidopsis. We show that patl1-2 and patl1-3, have a short root hair phenotype and that both mutant alleles exhibit a long root phenotype characterized by longer cells in the root elongation zone. Furthermore, we show that PATL1 colocalizes with VTI13-containing early endosomes in Arabidopsis seedlings roots. We are currently testing whether PATL1 may be recycled from VTI13 endosomes back to the plasma membrane.
Primary Faculty Mentor Name
Mary Tierney
Status
Graduate
Student College
College of Agriculture and Life Sciences
Program/Major
Plant Biology
Primary Research Category
Life Sciences
Unraveling the Role of Patellin1 in Expansive and Polarized Cell Growth
The Patellin gene family, a subgroup of Sec14-like proteins containing lipid binding domains, has been shown to play a role in membrane trafficking in Arabidopsis. The family members PATL3 and PATL6 have been implicated in impeding viral movement by binding to viral movement proteins (Peiro et al., 2014) . In addition, the patl2 patl4 patl5 patl6 quadruplet mutant, is defective in recycling of the auxin transport proteins PIN1 and PIN2 (Tejos et al., 2018). PATL1 localizes to the cell plate and the plasma membrane, and this is thought to be facilitated through its affinity for specific species of phosphoinositides (Peterman et al., 2004). We have characterized PATL1's involvement in expansive and polarized growth by examining two T-DNA null alleles (patl1-2 and patl1-3) in Arabidopsis. We show that patl1-2 and patl1-3, have a short root hair phenotype and that both mutant alleles exhibit a long root phenotype characterized by longer cells in the root elongation zone. Furthermore, we show that PATL1 colocalizes with VTI13-containing early endosomes in Arabidopsis seedlings roots. We are currently testing whether PATL1 may be recycled from VTI13 endosomes back to the plasma membrane.