Expression of the sarco/endoplasmic Ca2+-ATPase, SERCA1a, in fibroblasts induces the formation of organelle membrane arrays

Biehn, Suzanne E.; Czymmek, Kirk J.; Leavens, Karla F.; Karin, Norman J.

doi:10.1016/j.yexcr.2003.08.016

Cited by 5 publications

(3 citation statements)

References 48 publications

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“…Localization of GFP-PLB and GFP-SERCA1a. To better address intracellular trafficking of PLB and SERCA in living myocytes, we transiently transfected C2C12 myoblasts with GFP-PLB or GFP-SERCA1a, essentially as described by Biehn et al (4). The distribution of GFP-PLB ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Cellular trafficking of phospholamban and formation of functional sarcoplasmic reticulum during myocyte differentiation

Stenoien¹,

Knyushko²,

Londono³

et al. 2007

American Journal of Physiology-Cell Physiology

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Phospholamban (PLB) associates with the Ca(2+)-ATPase in sarcoplasmic reticulum (SR) membranes to permit the modulation of contraction in response to beta-adrenergic signaling. To understand how coordinated changes in the abundance and intracellular trafficking of PLB and the Ca(2+)-ATPase contribute to the maturation of functional muscle, we measured changes in abundance, location, and turnover of endogenous and tagged proteins in myoblasts and during their differentiation. We found that PLB is constitutively expressed in both myoblasts and differentiated myotubes, whereas abundance increases of the Ca(2+)-ATPase coincide with the formation of differentiated myotubes. We observed that PLB is primarily present in highly mobile vesicular structures outside the endoplasmic reticulum, irrespective of the expression of the Ca(2+)-ATPase, indicating that PLB targeting is regulated through vesicle trafficking. Moreover, using pulse-chase methods, we observed that in myoblasts, PLB is trafficked through directed transport through the Golgi to the plasma membrane before endosome-mediated internalization. The observed trafficking of PLB to the plasma membrane suggests an important role for PLB during muscle differentiation, which is distinct from its previously recognized role in the regulation of the Ca(2+)-ATPase.

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Section: Resultsmentioning

confidence: 99%

Cellular trafficking of phospholamban and formation of functional sarcoplasmic reticulum during myocyte differentiation

Stenoien¹,

Knyushko²,

Londono³

et al. 2007

American Journal of Physiology-Cell Physiology

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“…The ER is an extraordinarily plastic organelle. Large scale proliferation and/or reorganization of ER membranes frequently occur when exogenous or ER resident proteins are expressed at high levels, due to as diverse mechanisms as membrane protein stockpiling, the accumulation of misfolded, nondegradable proteins leading to aggresomes and Russel bodies, or lumenal osmotic changes (1,45–49). Accordingly, one has to be extremely careful in proposing an ER morphogenetic function for a protein solely based on its overexpression.…”

Section: Newcomers Proposed To Mediate Er–mt Interactionmentioning

confidence: 99%

Morphogenesis of the Endoplasmic Reticulum: Beyond Active Membrane Expansion

Vedrenne

Hauri

2006

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The endoplasmic reticulum (ER) of higher eukaryotic cells is a dynamic network of interconnected membrane tubules that pervades almost the entire cytoplasm. On the basis of the morphological changes induced by the disruption of the cytoskeleton or molecular motor proteins, the commonly accepted model has emerged that microtubules and conventional kinesin (kinesin-1) are essential determinants in establishing and maintaining the structure of the ER by active membrane expansion. Surprisingly, very similar ER phenotypes have now been observed when the cytoskeleton-linking ER membrane protein of 63 kDa (CLIMP-63) is mutated, revealing stable attachment of ER membranes to the microtubular cytoskeleton as a novel requirement for ER maintenance. Additional recent findings suggest that ER maintenance also requires ongoing homotypic membrane fusion, possibly controlled by the p97/p47/VICP135 protein complex. Work on other proteins proposed to regulate ER structure, including huntingtin, the EF-hand Ca 2þ -binding protein p22, the vesicle-associated membrane protein-associated protein B and kinectin isoforms further contribute to the new emerging concept that ER shape is not only determined by motor driven processes but by a variety of different mechanisms. Endoplasmic Reticulum -Microtubule ConnectionThe endoplasmic reticulum (ER) is a membrane-bound organelle present in all eukaryotic cells. It synthesizes lipids as well as secretory and membrane proteins, and ensures subsequent post-translational processing and quality control of the proteins (1-3). In addition, the ER is a multifunctional signaling organelle that controls entry and release of calcium, sterol biosynthesis, apoptosis and the release of arachidonic acid (4). The ER of higher eukaryotes comprises three main subdomains: the nuclear envelope, the ribosome-bound rough ER and the ribosome-free smooth ER. Both the absolute and relative abundance of rough and smooth ER varies with the cell type. ER membranes form flattened sheets, cisternae and tubules. In well-spread areas of the cell periphery, these tubules can be seen using light microscopy to form an irregular polygonal network with characteristic three-way junctions (5-7). Despite its complex organization, the ER is a continuous membrane compartment (8). The function of the cytoskeleton in ER architecture has been investigated in numerous studies, which revealed that microtubules (MTs) and ER are highly interdependent structures. Accordingly, the ER network retracts to the cell center in a number of experimental conditions that affect MTs or MT-associated proteins. These conditions include the depolymerization of the MT cytoskeleton by drugs or low temperature (9), the suppression of the heavy chain of the MT plus-end-directed motor protein kinesin (10) and the overexpression of the MT-associated protein tau that probably impedes kinesin-mediated transport (11). In addition, the extension of ER membranes along MTs has been imaged using video microscopy both in vivo (12) and in cell-free systems, where thi...

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“…However, this could lead to the dilution of ER shaping proteins (e.g., reticulons, atlastins, or members of the Lunapark family) if the expression of those are not upregulated in tandem. In a study using mouse fibroblasts, OSER-induction did not increase endogenous ER protein levels, also suggesting that this dilution of ER shaping proteins is likely (Biehn et al, 2004). The effects of reducing the relative concentrations of these ER shaping proteins have been observed in Arabidopsis following de-repression of ER membrane biosynthesis, which caused massive membrane proliferation, and transformed most of the ER into sheets (Eastmond et al, 2010).…”

Section: Current Understanding Of the Mechanism Of Oser Formationmentioning

confidence: 99%

IntEResting structures: formation and applications of organized smooth endoplasmic reticulum in plant cells

2020

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Expression of the sarco/endoplasmic Ca2+-ATPase, SERCA1a, in fibroblasts induces the formation of organelle membrane arrays

Cited by 5 publications

References 48 publications

Cellular trafficking of phospholamban and formation of functional sarcoplasmic reticulum during myocyte differentiation

Cellular trafficking of phospholamban and formation of functional sarcoplasmic reticulum during myocyte differentiation

Morphogenesis of the Endoplasmic Reticulum: Beyond Active Membrane Expansion

IntEResting structures: formation and applications of organized smooth endoplasmic reticulum in plant cells

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