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From the book SNARE Proteins

The SNARE Proteins of Green Plants

Anton Sanderfoot, Miyo Terao Morita and Masao Tasaka

Green plants are a significant part of our ecosystem and one of the primary food sources for mammals. Most likely, you experience a plant at some point every day: whether it is on a plate during diner, in a pot or a vase on your table, or under the shade of a tree. Like ourselves and our animal cousins, plants are a complex multicellular organism with specialized tissues and organs. Also like us, plants evolved these complicated multicellular tissues and organs from a unicellular ancestor; a unicellular ancestor that was different than the one we descend from. Nonetheless, those ancestors were both eukaryotes and already had the foundations of the complicated vesicle trafficking systems (and the complicated vesicle trafficking machinery!) of the multicellular descendants that followed. In the last few years, a great deal of research has begun to investigate the cell biology of the vesicle trafficking machinery of this other great multicellular lineage of organisms. This chapter will discuss the SNAREs of the green plants. In particular, we will focus on how plants have shaped the same core set of SNARE proteins inherited from the shared eukaryotic ancestor, how the expansion of the gene families of SNARE proteins may parallel the advent of multicellularity and how the SNARE proteins are intimately tied to essential physiology and behaviors in plants.
  • ISBN: TBA
  • Publication date: June 1, 2010
  • Series: Intelligence Unit
Taken from the book

SNARE Proteins

Edited by: Francesco Filippini and David Banfield

More chapters from the book:

Evolution of the SNARE Protein Superfamily

Evolving the SNARE proteins would have been an important innovation for the earliest eukaryotes. Genomic, phylogenetic and molecular cell biological studies from diverse eukaryotes have provided insight into both the general function and evolution of SNAREs. Here I review both the methodology and...

SNARE Function and Fatty Acids
Emma Connell, Frédéric Darios and Bazbek Davletov

Vesicle fusion is a ubiquitous biological process involved in membrane trafficking and a variety of specialised events such as exocytosis and neurite outgrowth. The energy to drive biological membrane fusion is provided by fusion proteins called SNAREs. Traditionally, studies have focused on the...

The SNARE Proteins of Green Plants
Anton Sanderfoot, Miyo Terao Morita and Masao Tasaka

Green plants are a significant part of our ecosystem and one of the primary food sources for mammals. Most likely, you experience a plant at some point every day: whether it is on a plate during diner, in a pot or a vase on your table, or under the shade of a tree. Like ourselves and our animal...

SNAREs in Cytokinesis
Kaajal Nagar and William S. Trimble

Cell division is a tightly regulated and complex multi‑step process requiring separation of duplicated chromosomes and division of the cytoplasm. During this process, a cell undergoes dramatic changes in both its shape and surface area. Cytokinesis, the process of separating the cytoplasm...

Mechanism of SNARE Assembly and Disassembly
Ulrike Winter and Dirk Fasshauer

The formation of SNARE (soluble NSF attachment protein receptor) complexes is the driving force for most types of biological membrane fusion reactions. An extremely fascinating feature of this reaction is its potency to couple the assembly energy to the mechanical process of pulling two membranes...

Structure of SNAREs
Axel T. Brunger

This review focuses on the structure of the so-called SNARE (Soluble N-ethyl maleimide sensitive factor Attachment Protein Receptors) proteins that are involved in exocytosis at the presynpatic plasma membrane. SNAREs exhibit multiple configurational, conformational and oliogomeric states. These...

SNARE Protein Effectors
Travis L. Rodkey and James McNew

SNARE proteins have been well characterized as the minimal machinery necessary for membrane fusion. SNARE‑mediated fusion at the plasma membrane begins with regulated formation of a t‑SNARE complex composed of syntaxin1A and SNAP25. This binary t‑SNARE complex can then bind to...

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