Tip-to-tip interaction in the crystal packing of PACSIN 2 is important in regulating tubulation activity
Protein & Cell
; (12): 695-701, 2013.
Article
ي En
| WPRIM
| ID: wpr-757771
المكتبة المسؤولة:
WPRO
ABSTRACT
The F-BAR domain containing proteins PACSINs are cytoplasmic phosphoproteins involved in various membrane deformations, such as actin reorganization, vesicle transport and microtubule movement. Our previous study shows that all PACSINs are composed of crescent shaped dimers with two wedge loops, and the wedge loop-mediated lateral interaction between neighboring dimers is important for protein packing and tubulation activity. Here, from the crystal packing of PACSIN 2, we observed a tight tip-to-tip interaction, in addition to the wedge loop-mediated lateral interaction. With this tip-to-tip interaction, the whole packing of PACSIN 2 shows a spiral-like assembly with a central hole from the top view. Elimination of this tip-to-tip connection inhibited the tubulation function of PACSIN 2, indicating that tip-to-tip interaction plays an important role in membrane deformation activity. Together with our previous study, we proposed a packing model for the assembly of PACSIN 2 on membrane, where the proteins are connected by tip-to-tip and wedge loop-mediated lateral interactions on the surface of membrane to generate various diameter tubules.
Key words
النص الكامل:
1
الفهرس:
WPRIM
الموضوع الرئيسي:
Recombinant Proteins
/
Models, Molecular
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Cell Membrane
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Chemistry
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Mutagenesis, Site-Directed
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Crystallography, X-Ray
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Protein Structure, Quaternary
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Adaptor Proteins, Signal Transducing
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Protein Interaction Domains and Motifs
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Static Electricity
المحددات:
Humans
اللغة:
En
مجلة:
Protein & Cell
السنة:
2013
نوع:
Article