This is a family of proteins widely distributed across the plant kingdom. Patellin (PATL) proteins are yeast Sec14 protein (Sec14p)-like phosphatidylinositol transfer proteins (PITPs) involved in several biological processes such as plant development and stress tolerance regulation, playing a role in membrane-trafficking events [, ]. In Arabidopsis, this family consists of six members, PATL1-6, and are characterised by the presence of two conserved domains observed in other membrane trafficking-related proteins: a Sec14p-like lipid-binding domain and a GOLD following the N-terminal variable domain. The GOLD domain is found in proteins related to Golgi function, membrane homeostasis and vesicle trafficking []. PATL1 is the defining member of this family, associated to the cell-plate, and has a regulatory role during cytokinesis, which is thought to be involved in clathrin-dependent endocytosis that aids cell plate remodeling and completion []. These proteins are able to interact with phosphoinositides, varying their affinity among them which results their involvement in different processes and signalling pathways. PATLs also respond to auxin and play a role in the regulation of PIN1, which suggests that they play a redundant and crucial role in polarity and patterning in Arabidopsis [, ].This entry also includes some CRAL-TRIO domain-containing proteins from fungi.
