Stacked Endoplasmic Reticulum Sheets Are Connected by Helicoidal Membrane Motifs

نویسندگان

  • Mark Terasaki
  • Tom Shemesh
  • Narayanan Kasthuri
  • Robin W. Klemm
  • Richard Schalek
  • Kenneth J. Hayworth
  • Arthur R. Hand
  • Maya Yankova
  • Greg Huber
  • Jeff W. Lichtman
  • Tom A. Rapoport
  • Michael M. Kozlov
چکیده

The endoplasmic reticulum (ER) often forms stacked membrane sheets, an arrangement that is likely required to accommodate a maximum of membrane-bound polysomes for secretory protein synthesis. How sheets are stacked is unknown. Here, we used improved staining and automated ultrathin sectioning electron microscopy methods to analyze stacked ER sheets in neuronal cells and secretory salivary gland cells of mice. Our results show that stacked ER sheets form a continuous membrane system in which the sheets are connected by twisted membrane surfaces with helical edges of left- or right-handedness. The three-dimensional structure of tightly stacked ER sheets resembles a parking garage, in which the different levels are connected by helicoidal ramps. A theoretical model explains the experimental observations and indicates that the structure corresponds to a minimum of elastic energy of sheet edges and surfaces. The structure allows the dense packing of ER sheets in the restricted space of a cell.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Gating Behavior of Endoplasmic Reticulum Potassium Channels of Rat Hepatocytes in Diabetes

Background: Defects in endoplasmic reticulum homeostasis are common occurrences in different diseases, such as diabetes, in which the function of endoplasmic reticulum is disrupted. It is now well established that ion channels of endoplasmic reticulum membrane have a critical role in endoplasmic reticulum luminal homeostasis. Our previous studies showed the presence of an ATP-sensitive cationic...

متن کامل

A model for the generation and interconversion of ER morphologies.

The peripheral endoplasmic reticulum (ER) forms different morphologies composed of tubules and sheets. Proteins such as the reticulons shape the ER by stabilizing the high membrane curvature in cross-sections of tubules and sheet edges. Here, we show that membrane curvature along the edge lines is also critical for ER shaping. We describe a theoretical model that explains virtually all observed...

متن کامل

Cytoplasmic acidification reduces potassium channel activities in the endoplasmic reticulum of rat hepatocytes

Introduction: Intracellular pH (pHi) regulates essentially all aspects of cellular activities. However, it is unknown how endoplasmic reticulum (ER) potassium channels sense pHi. In this study, we investigate the direct effects of pHi on ER potassium channels. Methods: We used channel incorporation into the bilayer lipid membrane method. L-α-phosphatidylcholine, a membrane lipid, was extrac...

متن کامل

An evidence for a potassium channel in endoplasmic reticulum based on single channel recording in bilayer lipid membrane

Introduction Numerous studies have demonstrated the presence of potassium selective channels in membranes internal organelles. These channels are essential to a large variety of cellular processes including intracellular 2+ a signaling, protein recycling, charge neutralization and cell protection. In contrast to the sarcoplasmic reticulum + here potassium channels have been clearly ...

متن کامل

Evidences on the existence of a new potassium channel in the rough endoplasmic reticulum (RER) of rat hepatocytes

Introduction: we have recently reported the presence of two potassium currents with 598 and 368 pS conductance in the rough endoplasmic reticulum (RER) membrane. The 598 pS channel was voltage dependent and ATP sensitive. However, the 368 pS channel was rarely observed and its identity remained obscure. Since cationic channels in intracellular organelles such as mitochondria and RER play imp...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Cell

دوره 154  شماره 

صفحات  -

تاریخ انتشار 2013