Home General Physiology and Biophysics 2014 General Physiology and Biophysics Vol.33, No.4, p.411–423, 2014

Journal info


Founded: 1982
ISSN 1338-4325 (online)
ISSN 0231-5882 (print)
Published in English,
6 times per year

Aims and Scope
Editorial Info
Submission Guidelines

Select Journal







Webshop Cart

Your Cart is currently empty.

Info: Your browser does not accept cookies. To put products into your cart and purchase them you need to enable cookies.

General Physiology and Biophysics Vol.33, No.4, p.411–423, 2014

Title: Spoke ring and anchorage of nuclear pore complex revealed by high resolution transmission electron microscopy
Author: Jarmil Prachař

Abstract:  Using several different methods, the nuclear pore complex (NPC) was shown to be anchored in the nuclear envelope into the specific curved region, called pore membrane. Three transmembrane nucleoporins in the equatorial region of NPC contain hydrophobic stretches, which exhibit the ability to intersect the phospholipid bilayer. Using transmission electron microscopy, we observed three different evaluable morphological situations in the section through the NPC spoke ring (SR). We suppose that some sections are directed through one type of subunit that is responsible for anchoring. Other sections are directed through the second type of subunit that may provide pore membrane bending. Finally, the spoke ring is sectioned between aforementioned subunits where the pore membrane is best preserved. The proposed anchor is represented by the chains of protein complexes which replace phospholipid bilayer in a relatively large area. Second subunit, presumed bending module is represented by the bundles of chains copying the shape of the pore membrane from the side of the NPC. This work is based on very high resolution resulting in unique and complicated images of tangled and cut off protein chains, nevertheless, it provides insight into how some proteins interact with or replace the membrane.

Keywords: Nuclear pore complex — Spoke ring — Anchorage — High resolution transmission electron microscopy
Year: 2014, Volume: 33, Issue: 4 Page From: 411, Page To: 423
doi:10.4149/gpb_2014013


download file



© AEPress s.r.o
Copyright notice: For any permission to reproduce, archive or otherwise use the documents in the ELiS, please contact AEP.