Role of plant lipid transfer proteins in plant cell physiology—A concise review

Peptides ◽  
2007 ◽  
Vol 28 (5) ◽  
pp. 1144-1153 ◽  
Author(s):  
André de Oliveira Carvalho ◽  
Valdirene Moreira Gomes

2020 ◽  
Vol 528 (1) ◽  
pp. 39-45 ◽  
Author(s):  
D.N. Melnikova ◽  
I.V. Bogdanov ◽  
A.A. Ignatova ◽  
T.V. Ovchinnikova ◽  
E.I. Finkina


2002 ◽  
Vol 357 (1423) ◽  
pp. 909-916 ◽  
Author(s):  
Dirk K. Hincha

Plants from temperate and cold climates are able to increase their freezing tolerance during exposure to low non–freezing temperatures. It has been shown that several genes are induced in a coordinated manner during this process of cold acclimation. The functional role of most of the corresponding cold–regulated proteins is not yet known. We summarize our knowledge of those cold–regulated proteins that are able to stabilize membranes during a freeze–thaw cycle. Special emphasis is placed on cryoprotectin, a lipid–transfer protein homologue that was isolated from cold–acclimated cabbage leaves and that protects isolated chloroplast thylakoid membranes from freeze–thaw damage.





2020 ◽  
Vol 133 (18) ◽  
pp. jcs247148 ◽  
Author(s):  
Alessandra Gallo ◽  
Lydia Danglot ◽  
Francesca Giordano ◽  
Bailey Hewlett ◽  
Thomas Binz ◽  
...  

ABSTRACTAxons and dendrites are long and often ramified neurites that need particularly intense plasma membrane (PM) expansion during the development of the nervous system. Neurite growth depends on non-fusogenic Sec22b–Stx1 SNARE complexes at endoplasmic reticulum (ER)–PM contacts. Here, we show that Sec22b interacts with members of the extended synaptotagmin (E-Syt) family of ER lipid transfer proteins (LTPs), and this interaction depends on the longin domain of Sec22b. Overexpression of E-Syts stabilizes Sec22b–Stx1 association, whereas silencing of E-Syts has the opposite effect. Overexpression of wild-type E-Syt2, but not mutants unable to transfer lipids or attach to the ER, increase the formation of axonal filopodia and ramification of neurites in developing neurons. This effect is inhibited by a clostridial neurotoxin cleaving Stx1, and expression of the Sec22b longin domain and a Sec22b mutant with an extended linker between the SNARE and transmembrane domains. We conclude that Sec22b–Stx1 ER–PM contact sites contribute to PM expansion by interacting with LTPs, such as E-Syts.This article has an associated First Person interview with the first author of the paper.



2002 ◽  
Vol 110 (5) ◽  
pp. 790-796 ◽  
Author(s):  
Araceli Díaz-Perales ◽  
Ana I. Tabar ◽  
Rosa Sánchez-Monge ◽  
Blanca E. García ◽  
Belén Gómez ◽  
...  


1995 ◽  
Vol 109 (2) ◽  
pp. 445-455 ◽  
Author(s):  
BPA. Cammue ◽  
K. Thevissen ◽  
M. Hendriks ◽  
K. Eggermont ◽  
I. J. Goderis ◽  
...  




2018 ◽  
Vol 58 (11) ◽  
pp. 2294-2304 ◽  
Author(s):  
Flávia Camila Vieira da Silva ◽  
Viviane Veiga do Nascimento ◽  
Olga Lima Tavares Machado ◽  
Lídia da Silva Pereira ◽  
Valdirene Moreira Gomes ◽  
...  


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