scholarly journals Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins

1998 ◽  
Vol 7 (12) ◽  
pp. 2490-2498 ◽  
Author(s):  
Mathilde H. Lerche ◽  
Flemming M. Poulsen
Keyword(s):  
Solution Structure ◽  
Lipid Transfer Protein ◽  
Binding Modes ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Transfer Protein

scholarly journals Multiple binding modes for palmitate to barley lipid transfer protein facilitated by the presence of proline 12

2012 ◽  
Vol 22 (1) ◽  
pp. 56-64 ◽  
Author(s):  
Lorna J. Smith ◽  
Wilfred F. Van Gunsteren ◽  
Jane R. Allison
Keyword(s):  
Lipid Transfer Protein ◽  
Binding Modes ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Multiple Binding

Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features

2005 ◽  
Vol 59 (2) ◽  
pp. 356-367 ◽  
Author(s):  
Pedro Da Silva ◽  
Céline Landon ◽  
Benoit Industri ◽  
Antoine Marais ◽  
Didier Marion ◽  
...  
Keyword(s):  
Solution Structure ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Biological Features

scholarly journals Movement of accessible plasma membrane cholesterol by the GRAMD1 lipid transfer protein complex

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Tomoki Naito ◽  
Bilge Ercan ◽  
Logesvaran Krshnan ◽  
Alexander Triebl ◽  
Dylan Hong Zheng Koh ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Intracellular Transport ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Transfer Protein ◽  
Major Structural Component ◽  
Acute Increase ◽  
Transport Transition ◽  
Plasma Membrane Cholesterol

Cholesterol is a major structural component of the plasma membrane (PM). The majority of PM cholesterol forms complexes with other PM lipids, making it inaccessible for intracellular transport. Transition of PM cholesterol between accessible and inaccessible pools maintains cellular homeostasis, but how cells monitor the accessibility of PM cholesterol remains unclear. We show that endoplasmic reticulum (ER)-anchored lipid transfer proteins, the GRAMD1s, sense and transport accessible PM cholesterol to the ER. GRAMD1s bind to one another and populate ER-PM contacts by sensing a transient expansion of the accessible pool of PM cholesterol via their GRAM domains. They then facilitate the transport of this cholesterol via their StART-like domains. Cells that lack all three GRAMD1s exhibit striking expansion of the accessible pool of PM cholesterol as a result of less efficient PM to ER transport of accessible cholesterol. Thus, GRAMD1s facilitate the movement of accessible PM cholesterol to the ER in order to counteract an acute increase of PM cholesterol, thereby activating non-vesicular cholesterol transport.

scholarly journals Solution Structure of Plant Nonspecific Lipid Transfer Protein-2 from Rice (Oryza sativa)

2002 ◽  
Vol 277 (38) ◽  
pp. 35267-35273 ◽  
Author(s):  
Dharmaraj Samuel ◽  
Yaw-Jen Liu ◽  
Chao-Sheng Cheng ◽  
Ping-Chiang Lyu
Keyword(s):  
Oryza Sativa ◽  
Solution Structure ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Nonspecific Lipid Transfer Protein

Solution structure of a lipid transfer protein extracted from rice seeds

2001 ◽  
Vol 259 (3) ◽  
pp. 692-708 ◽  
Author(s):  
Jarek Poznanski ◽  
Patrick Sodano ◽  
Se Won Suh ◽  
Jae Young Lee ◽  
Marius Ptak ◽  
...  
Keyword(s):  
Solution Structure ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Rice Seeds

scholarly journals Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds

1996 ◽  
Vol 5 (4) ◽  
pp. 565-577 ◽  
Author(s):  
Jérôme Gomar ◽  
Marie-Christine Petit ◽  
Patrick Sodano ◽  
Denise Sy ◽  
Didier Marion ◽  
...  
Keyword(s):  
Solution Structure ◽  
Lipid Transfer Protein ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Maize Seeds ◽  
Nonspecific Lipid Transfer Protein

scholarly journals A model for a partnership of lipid transfer proteins and scramblases in membrane expansion and organelle biogenesis

2021 ◽  
Vol 118 (16) ◽  
pp. e2101562118
Author(s):  
Alireza Ghanbarpour ◽  
Diana P. Valverde ◽  
Thomas J. Melia ◽  
Karin M. Reinisch
Keyword(s):  
Lipid Transfer Protein ◽  
Membrane Dynamics ◽  
Lipid Homeostasis ◽  
In Vitro Assays ◽  
Lipid Transfer ◽  
Organelle Biogenesis ◽  
Lipid Transfer Proteins ◽  
Transfer Protein ◽  
Donor And Acceptor

The autophagy protein ATG2, proposed to transfer bulk lipid from the endoplasmic reticulum (ER) during autophagosome biogenesis, interacts with ER residents TMEM41B and VMP1 and with ATG9, in Golgi-derived vesicles that initiate autophagosome formation. In vitro assays reveal TMEM41B, VMP1, and ATG9 as scramblases. We propose a model wherein membrane expansion results from the partnership of a lipid transfer protein, moving lipids between the cytosolic leaflets of apposed organelles, and scramblases that reequilibrate the leaflets of donor and acceptor organelle membranes as lipids are depleted or augmented. TMEM41B and VMP1 are implicated broadly in lipid homeostasis and membrane dynamics processes in which their scrambling activities likely are key.

scholarly journals A lipid transfer protein that transfers lipid

2007 ◽  
Vol 179 (1) ◽  
pp. 11-13 ◽  
Author(s):  
Tim P. Levine
Keyword(s):  
Lipid Transfer Protein ◽  
Adaptor Protein ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Transfer Protein ◽  
Cell Biol ◽  
Circuitous Route

Very few lipid transfer proteins (LTPs) have been caught in the act of transferring lipids in vivo from a donor membrane to an acceptor membrane. Now, two studies (Halter, D., S. Neumann, S.M. van Dijk, J. Wolthoorn, A.M. de Maziere, O.V. Vieira, P. Mattjus, J. Klumperman, G. van Meer, and H. Sprong. 2007. J. Cell Biol. 179:101–115; D'Angelo, G., E. Polishchuk, G.D. Tullio, M. Santoro, A.D. Campli, A. Godi, G. West, J. Bielawski, C.C. Chuang, A.C. van der Spoel, et al. 2007. Nature. 449:62–67) agree that four-phosphate adaptor protein 2 (FAPP2) transfers glucosylceramide (GlcCer), a lipid that takes an unexpectedly circuitous route.

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