Title

Patellin1, a novel Sec14-like protein, localizes to the cell plate and binds phosphoinositides

UMMS Affiliation

Department of Cell Biology

Date

10-7-2004

Document Type

Article

Subjects

Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Gene Expression Regulation, Plant; Microscopy, Fluorescence; Molecular Sequence Data; Multigene Family; Phosphatidylinositols; Phospholipid Transfer Proteins; Plant Roots; Protein Binding; Sequence Alignment; Sequence Homology, Amino Acid; Tobacco

Disciplines

Cell Biology | Life Sciences | Medicine and Health Sciences

Abstract

Membrane trafficking is central to construction of the cell plate during plant cytokinesis. Consequently, a detailed understanding of the process depends on the characterization of molecules that function in the formation, transport, targeting, and fusion of membrane vesicles to the developing plate, as well as those that participate in its consolidation and maturation into a fully functional partition. Here we report the initial biochemical and functional characterization of patellin1 (PATL1), a novel cell-plate-associated protein that is related in sequence to proteins involved in membrane trafficking in other eukaryotes. Analysis of the Arabidopsis genome indicated that PATL1 is one of a small family of Arabidopsis proteins, characterized by a variable N-terminal domain followed by two domains found in other membrane-trafficking proteins (Sec14 and Golgi dynamics domains). Results from immunolocalization and biochemical fractionation studies suggested that PATL1 is recruited from the cytoplasm to the expanding and maturing cell plate. In vesicle-binding assays, PATL1 bound to specific phosphoinositides, important regulators of membrane trafficking, with a preference for phosphatidylinositol(5)P, phosphatidylinositol(4,5)P(2), and phosphatidylinositol(3)P. Taken together, these findings suggest a role for PATL1 in membrane-trafficking events associated with cell-plate expansion or maturation and point to the involvement of phosphoinositides in cell-plate biogenesis.

Rights and Permissions

Citation: Plant Physiol. 2004 Oct;136(2):3080-94; discussion 3001-2. Epub 2004 Oct 1. Link to article on publisher's site

Related Resources

Link to article in PubMed

PubMed ID

15466235