scholarly journals Who plays the ferryman: ATG2 channels lipids into the forming autophagosome

2019 ◽  
Vol 218 (6) ◽  
pp. 1767-1768 ◽  
Author(s):  
Nicholas T. Ktistakis
Keyword(s):  
Membrane Proteins ◽  
Lipid Transfer Protein ◽  
Protein Family ◽  
Lipid Transfer ◽  
Related Protein ◽  
Transfer Protein ◽  
Cell Biol

Expansion of the autophagosomal membrane requires a mechanism to supply lipids while excluding most membrane proteins. In this issue, Valverde et al. (2019. J. Cell Biol. https://doi.org/10.1083/jcb.201811139) identify ATG2, a member of the autophagy-related protein family, as a lipid transfer protein and provide important novel insights on how autophagosomes grow.

scholarly journals cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family

2002 ◽  
Vol 32 (9) ◽  
pp. 1387-1387 ◽  
Author(s):  
A. Diaz-Perales ◽  
G. Garcia-Casado ◽  
R. Sanchez-Monge ◽  
F. J. Garcia-Selles ◽  
D. Barber ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Cdna Cloning ◽  
Lipid Transfer Protein ◽  
Protein Family ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Major Allergens

scholarly journals Lipid transfer particle from the silkworm,Bombyx mori, is a novel member of the apoB/large lipid transfer protein family

2013 ◽  
Vol 54 (9) ◽  
pp. 2379-2390 ◽  
Author(s):  
Hiroshi Yokoyama ◽  
Takeru Yokoyama ◽  
Masashi Yuasa ◽  
Hirofumi Fujimoto ◽  
Takashi Sakudoh ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Lipid Transfer Protein ◽  
Protein Family ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Silkworm Bombyx Mori

scholarly journals Identification and analysis of non-specific lipid transfer protein family in tobacco

2021 ◽  
Vol 47 (11) ◽  
pp. 2184-2198
Author(s):  
Peng LI ◽  
Che LIU ◽  
Hao SONG ◽  
Pan-Pan YAO ◽  
Pei-Lin SU ◽  
...  
Keyword(s):  
Lipid Transfer Protein ◽  
Protein Family ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid

scholarly journals VPS13: A lipid transfer protein making contacts at multiple cellular locations

2018 ◽  
Vol 217 (10) ◽  
pp. 3322-3324 ◽  
Author(s):  
Mingming Gao ◽  
Hongyuan Yang
Keyword(s):  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Cell Biol ◽  
Evolutionarily Conserved ◽  
Membrane Contact

The evolutionarily conserved VPS13 proteins localize to multiple membrane contact sites though their function and regulation has been elusive. Bean et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201804111) found that competitive adaptors control the different localizations of yeast Vps13p, while Kumar et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201807019) provide biochemical and structural evidence for VPS13 proteins in the nonvesicular transport of phospholipids.

cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family

2002 ◽  
Vol 32 (1) ◽  
pp. 87-92 ◽  
Author(s):  
A. Diaz-Perales ◽  
G. Garcia-Casado ◽  
R. Sanchez-Monge ◽  
F. J. Garcia-Selles ◽  
D. Barber ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Cdna Cloning ◽  
Lipid Transfer Protein ◽  
Protein Family ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Major Allergens

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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