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ArtikelAggregation and vesiculation of membrane proteins by curvature-mediated interactions  
Oleh: Reynwar, Benedict J. ; lllya, Gregoria ; Harmandaris, Vagelis A. ; Muller, Martin M. ; Kremer, Kurt ; Deserno, Markus
Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: NATURE (keterangan: ada di Proquest) vol. 447 no. 7143 (May 2007), page 461.
Ketersediaan
  • Perpustakaan FK
    • Nomor Panggil: N01.K.2007.05
    • Non-tandon: 1 (dapat dipinjam: 0)
    • Tandon: tidak ada
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Isi artikelMembrane remodelling'-S plays an important role in cellular tasks such as endocytosis, vesiculation and protein sorting, and in the biogenesis of organelles such as the endoplasmic reticulum or the Golgi apparatus. It is well established that the remodelling process is aided by specialized proteins that can sense4 as well as create6 membrane curvature, and trigger tubulation7-9 when added to synthetic liposomes. Because the energy needed for such largescale changes in membrane geometry significantly exceeds the binding energy between individual proteins and between protein and membrane, cooperative action is essential. It has recently ~n suggested'o,,, that curvature-mediated attractive interactions could aid cooperation and complement the effects of specific binding events on membrane remodelling. But it is difficult to experimentally isolate curvature-mediated interactions from direct attractions between proteins. Moreover, approximate theories predict repulsion between isotropically curving proteins12-15. Here we use coarse-grained membrane simulations to show that curvature-inducing model proteins adsorbed on lipid bilayer membranes can experience attractive interactions that arise purely as a result of membrane curvature. We find that once a minimal local bending is realized, the effect robustly drives protein cluster formation and subsequent transformation into vesicles with radii that correlate with the local curvature imprint. Owing to its universal nature, curvature-mediated attraction can operate even between proteins lacking any specific interactions, such as newly synthesized and still immature membrane proteins in the endoplasmic reticulum.
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