Anton A. Sanderfoot

University of Wisconsin–La Crosse

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Natasha V. Raikhel

University of California, Riverside

Scott Cooper

University of Wisconsin–La Crosse

Sondra G. Lazarowitz

Cornell University

Diane C. Bassham

St Martins Hospital

Asaf Salamov

Joint Genome Institute

Igor V. Grigoriev

University of California, Berkeley

Francis Marty

Université de Bourgogne

Susan K. Dutcher

Washington University in St. Louis

Harris Shapiro

Joint Genome Institute

Astrid Terry

University of Glasgow

Cooperative Institutions

Joint Genome Institute

115

Institut de Biologie Physico-Chimique

Sorbonne Université

Centre National de la Recherche Scientifique

Duke University

Lawrence Berkeley National Laboratory

University of Massachusetts Chan Medical School

University of California, Los Angeles

Kanazawa University

Lawrence Livermore National Laboratory

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The localization of AtPEP12, a syntaxin homolog, during different stages of plant development

Biology of the Cell (1998)

Alexande Silva da Conceicao Danièle Marty‐Mazars Sandra Arrault Anton A. Sanderfoot Hanna Levanony

10.1016/s0248-4900(98)80294-3

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Citations (0)

Predictions from Sequence

Springer eBooks (2018)

Scott Cooper Anton A. Sanderfoot

Sequence (biology)

10.1007/978-1-4614-1531-2_7

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Citations (0)

...response: Uncoating the pathway to the vacuole in Arabidopsis

Trends in Plant Science (1999)

Anton A. Sanderfoot Natasha V. Raikhel

Plant cell

Cotyledon

10.1016/s1360-1385(98)01366-1

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Interactions between Syntaxins Identify at Least Five SNARE Complexes within the Golgi/Prevacuolar System of the Arabidopsis Cell

Molecular Biology of the Cell (2001)

Anton A. Sanderfoot Valya Kovaleva Diane C. Bassham Natasha V. Raikhel

The syntaxin family of soluble N-ethyl maleimide sensitive factor adaptor protein receptors (SNAREs) is known to play an important role in the fusion of transport vesicles with specific organelles. Twenty-four syntaxins are encoded in the genome of the model plant Arabidopsis thaliana. These 24 genes are found in 10 gene families and have been reclassified as syntaxins of plants (SYPs). Some of these gene families have been previously characterized, with the SYP2-type syntaxins being found in the prevacuolar compartment (PVC) and the SYP4-type syntaxins on thetrans-Golgi network (TGN). Here we report on two previously uncharacterized syntaxin groups. The SYP5 group is encoded by a two-member gene family, whereas SYP61 is a single gene. Both types of syntaxins are localized to multiple compartments of the endomembrane system, including the TGN and the PVC. These two groups of syntaxins form SNARE complexes with each other, and with other Arabidopsis SNAREs. On the TGN, SYP61 forms complexes with the SNARE VTI12 and either SYP41 or SYP42. SYP51 and SYP61 interact with each other and with VTI12, most likely also on the TGN. On the PVC, a SYP5-type syntaxin interacts specifically with a SYP2-type syntaxin, as well as the SNARE VTI11, forming a SNARE complex likely involved in TGN-to-PVC trafficking.

Syntaxin 3

SNARE complex

Endomembrane system

10.1091/mbc.12.12.3733

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Citations (259)

A Viral Movement Protein as a Nuclear Shuttle (The Geminivirus BR1 Movement Protein Contains Domains Essential for Interaction with BL1 and Nuclear Localization)

PLANT PHYSIOLOGY (1996)

Anton A. Sanderfoot David J. Ingham Sondra G. Lazarowitz

For the nuclear replicating bipartite geminiviruses such as squash leaf curl to systemically infect the host requires the active participation of two virus-encoded movement proteins, BR1 and BL1. These act in a cooperative manner to transport the viral single-stranded DNA genome from its site of replication in the nucleus to the cell periphery (A.A. Sanderfoot, S.G. Lazarowitz [1995] Plant Cell 7: 1185-1194). We have proposed that BR1 functions as a nuclear shuttle protein, transporting the viral single-stranded DNA to and from the nucleus as a complex that is recognized by BL1 for movement to adjacent cells. To further investigate this, we expressed BR1 mutants known to affect viral infectivity in Spodoptera frugiperda insect cells and Nicotiana tabacum L. cv Xanthi protoplasts and found these to be defective in either their nuclear targeting or their ability to be redirected to the cell periphery when co-expressed with BL1. Translational fusions to beta-glucuronidase and alanine-scanning mutagenesis further demonstrated that the C-terminal 86 amino acids of BR1 contains a domain(s) essential for its interaction with BL1 and identified two nuclear localization signals within the N-terminal 113 residues of BR1. These nuclear localization signals were precisely located within distinct 16- and 22-peptide segments of BR1. These studies support and extend our model for squash leaf curl virus movement, showing that BR1 has a domain structure, with an N-terminal region required for nuclear targeting and a C-terminal region required for its interaction with BL1.

NLS

Movement protein

Sf9

Plasmodesma

Alanine scanning

10.1104/pp.110.1.23

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Citations (151)

Predictions from Sequence

Springer eBooks (2014)

Scott Cooper Anton A. Sanderfoot

Sequence (biology)

10.1007/978-1-4614-6436-5_7-3

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Citations (0)

The Specificity of Vesicle Trafficking: Coat Proteins and SNAREs

The Plant Cell (1999)

Anton A. Sanderfoot Natasha V. Raikhel

Proteins that are destined for the secretory system usually begin their journey at the endoplasmic reticulum (ER), where proteins are translocated across the ER membrane into the lumen, before being selectively removed from the ER and packaged as cargo into transport vesicles bound for the stacks of

Secretory protein

Lumen (anatomy)

COPII

Secretory Vesicle

Transport protein

Vesicular Transport Proteins

10.1105/tpc.11.4.629

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Citations (163)

Building the Impetus for Change: An Across-Curriculum Initiative in Biology

Journal of College Science Teaching (2015)

Gretchen A. Gerrish Anton A. Sanderfoot Tisha C. King‐Heiden Mike Abler Kathryn E. Perez

10.2505/4/jcst15_044_04_28

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Citations (2)

NPSN11 Is a Cell Plate-Associated SNARE Protein That Interacts with the Syntaxin KNOLLE

PLANT PHYSIOLOGY (2002)

Haiyan Zheng Sebastian Y. Bednarek Anton A. Sanderfoot José M. Alonso Joseph R. Ecker

Abstract SNAREs are important components of the vesicle trafficking machinery in eukaryotic cells. In plants, SNAREs have been found to play a variety of roles in the development and physiology of the whole organism. Here, we describe the identification and characterization of a novel plant-specific SNARE, NPSN11, a member of a closely related small gene family in Arabidopsis. NSPN11 is highly expressed in actively dividing cells. In a subcellular fractionation experiment, NSPN11 cofractionates with the cytokinesis-specific syntaxin, KNOLLE, which is required for the formation of the cell plate. By immunofluorescence microscopy, NSPN11 was localized to the cell plate in dividing cells. Consistent with the localization studies, NSPN11 was found to interact with KNOLLE. Our results suggest that NPSN11 is another component of the membrane trafficking and fusion machinery involved in cell plate formation.

Cell fractionation

Cell plate

SNARE complex

10.1104/pp.003970

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Citations (92)

The Physcomitrella Genome Reveals Evolutionary Insights into the Conquest of Land by Plants

Science (2007)

Stefan A. Rensing Daniel Lang Andreas Zimmer Astrid Terry Asaf Salamov

We report the draft genome sequence of the model moss Physcomitrella patens and compare its features with those of flowering plants, from which it is separated by more than 400 million years, and unicellular aquatic algae. This comparison reveals genomic changes concomitant with the evolutionary movement to land, including a general increase in gene family complexity; loss of genes associated with aquatic environments (e.g., flagellar arms); acquisition of genes for tolerating terrestrial stresses (e.g., variation in temperature and water availability); and the development of the auxin and abscisic acid signaling pathways for coordinating multicellular growth and dehydration response. The Physcomitrella genome provides a resource for phylogenetic inferences about gene function and for experimental analysis of plant processes through this plant's unique facility for reverse genetics.

Physcomitrella patens

Multicellular organism

plant evolution

10.1126/science.1150646

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Citations (1,775)