The presence of an ER exit signal determines the protein sorting upon ER exit in yeast

2008 ◽  
Vol 414 (2) ◽  
pp. 237-245 ◽  
Author(s):  
Reika Watanabe ◽  
Guillaume A. Castillon ◽  
Anja Meury ◽  
Howard Riezman
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Sorting ◽  
Surface Protein ◽  
The Other ◽  
Gpi Anchor ◽  
Rich Region ◽  
Characteristic Features ◽  
Detergent Resistant Membrane

In yeast, there are at least two vesicle populations upon ER (endoplasmic reticulum) exit, one containing Gap1p (general aminoacid permease) and a glycosylated α-factor, gpαF (glycosylated proα-factor), and the other containing GPI (glycosylphosphatidylinositol)-anchored proteins, Gas1p (glycophospholipid-anchored surface protein) and Yps1p. We attempted to identify sorting determinants for this protein sorting event in the ER. We found that mutant Gas1 proteins that lack a GPI anchor and/or S/T region (serine- and threonine-rich region), two common characteristic features conserved among yeast GPI-anchored proteins, were still sorted away from Gap1p-containing vesicles. Furthermore, a mutant glycosylated α-factor, gpαGPI, which contains both the GPI anchor and S/T region from Gas1p, still entered Gap1p-containing vesicles, demonstrating that these conserved characteristics do not prevent proteins from entering Gap1p-containing vesicles. gpαF showed severely reduced budding efficiency in the absence of its ER exit receptor Erv29p, and this residual budding product no longer entered Gap1p-containing vesicles. These results suggest that the interaction of gpαF with Erv29p is essential for sorting into Gap1p-containing vesicles. We compared the detergent solubility of Gas1p and the gpαGPI in the ER with that in ER-derived vesicles. Both GPI-anchored proteins similarly partitioned into the DRM (detergent-resistant membrane) in the ER. Based on the fact that they entered different ER-derived vesicles, we conclude that DRM partitioning of GPI-anchored proteins is not the dominant determinant of protein sorting upon ER exit. Interestingly, upon incorporation into the ER-derived vesicles, gpαGPI was no longer detergent-insoluble, in contrast with the persistent detergent insolubility of Gas1p in the ER-derived vesicles. We present different explanations for the different behaviours of GPI-anchored proteins in distinct ER-derived vesicle populations.

scholarly journals Cantharidin alters GPI-anchored protein sorting by targeting Cdc1 mediated remodeling in Endoplasmic Reticulum

2018 ◽  
Author(s):  
Pushpendra Kumar Sahu ◽  
Raghuvir Singh Tomar
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Genetic Interaction ◽  
Protein Sorting ◽  
Model Organism ◽  
Cell Wall Integrity ◽  
Yeast Cells ◽  
Growth Media ◽  
Gpi Anchor ◽  
Associated Functions

ABSTRACTCantharidin (CTD) is a potent anticancer small molecule produced by several species of blister beetle. It has been a traditional medicine for the treatment of warts and tumors for many decades. CTD suppresses the tumor growth by inducing apoptosis, cell cycle arrest, and DNA damage. It is a known inhibitor of PP2A and PP1. In this study, we identified new molecular targets of CTD usingSaccharomyces cerevisiaeas a model organism which expresses a Cantharidin Resistance Gene (CRG1).CRG1encodes a SAM-dependent methyltransferase that inactivates CTD by methylation. CTD alters lipid homeostasis, cell wall integrity, endocytosis, adhesion, and invasion in yeast cells. We found that CTD specifically affects the phosphatidylethanolamine (PE) associated functions which can be rescued by supplementation of ethanolamine (ETA) in the growth media. CTD also perturbed ER homeostasis and cell wall integrity by altering the GPI-anchored protein sorting. The CTD dependent genetic interaction profile ofCRG1revealed that Cdc1 activity in GPI-anchor remodeling is the key target of CTD, which we found to be independent of PP2A and PP1. Furthermore, our experiments with human cells suggest that CTD functions through a conserved mechanism in higher eukaryotes as well. Altogether, we conclude that CTD induces cytotoxicity by targeting Cdc1 activity in GPI-anchor remodeling in the endoplasmic reticulum (ER).

Compound Symbiosis in Peridinium Balticum

1973 ◽  
Vol 31 ◽  
pp. 500-501
Author(s):  
R. N. Tomas
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
The Other ◽  
Exact Nature ◽  
Symbiotic Relationship

Peridinium balticum appears to be unusual among the dinoflagellates in that it possesses two DNA-containing structures as determined by histochemical techniques. Ultrastructurally, the two dissimilar nuclei are contained within different protoplasts; one of the nuclei is characteristically dinophycean in nature, while the other is characteristically eucaryotic. The chloroplasts observed within P. balticum are intrinsic to an eucaryotic photosynthetic endosymbiont and not to the dinoflagellate. These organelles are surrounded by outpocketings of endoplasmic reticulum which are continuous with the eucaryotic nuclear envelope and are characterized by thylakoids composed of three apposed lamellae. Girdle lamellae and membranebounded interlamellar pyrenoids are also present. Only the plasmalemma of the endosymbiont segregates its protoplast from that of the dinophycean cytoplasm. The exact nature of this symbiotic relationship is at present not known.

Golgi Apparatus and Melanogenesis: Ultrastructural Study of a Human Cellular Blue Nevus (Melanocytoma)

1973 ◽  
Vol 31 ◽  
pp. 380-381
Author(s):  
S.R. Allegra
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Ultrastructural Study ◽  
The Other ◽  
Blue Nevus ◽  
Normal Complement ◽  
Golgi Vesicles ◽  
Golgi System ◽  
The Subject ◽  
Cellular Blue Nevus

The respective roles of the ribo somes, endoplasmic reticulum, Golgi apparatus and perhaps nucleus in the synthesis and maturation of melanosomes is still the subject of some controversy. While the early melanosomes (premelanosomes) have been frequently demonstrated to originate as Golgi vesicles, it is undeniable that these structures can be formed in cells in which Golgi system is not found. This report was prompted by the findings in an essentially amelanotic human cellular blue nevus (melanocytoma) of two distinct lines of melanocytes one of which was devoid of any trace of Golgi apparatus while the other had normal complement of this organelle.

Tolerance is theoretical and practical principles

1996 ◽  
pp. 13-23
Author(s):  
Mykhailo Babiy
Keyword(s):  
Religious Diversity ◽  
The Other ◽  
Nodal Points ◽  
Characteristic Features ◽  
The One ◽  
Ukrainian Society

Political ideological pluralism, religious diversity are characteristic features of modern Ukrainian society. On the one hand, multiculturalism, socio-political, religious differentiation of the latter appear as important characteristics of its democracy, as a practical expression of freedom, on the other - as a factor that led to the deconsocialization of society, gave rise to "nodal points" of tension, confrontational processes, in particular, in political and religious spheres.

scholarly journals Ceramide chain length–dependent protein sorting into selective endoplasmic reticulum exit sites

2020 ◽  
Vol 6 (50) ◽  
pp. eaba8237
Author(s):  
Sofia Rodriguez-Gallardo ◽  
Kazuo Kurokawa ◽  
Susana Sabido-Bozo ◽  
Alejandro Cortes-Gomez ◽  
Atsuko Ikeda ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Chain Length ◽  
Secretory Pathway ◽  
Protein Sorting ◽  
Endoplasmic Reticulum Membrane ◽  
Lipid Chain ◽  
Secretory Transport ◽  
Dependent Protein ◽  
Cellular Compartmentalization

Protein sorting in the secretory pathway is crucial to maintain cellular compartmentalization and homeostasis. In addition to coat-mediated sorting, the role of lipids in driving protein sorting during secretory transport is a longstanding fundamental question that still remains unanswered. Here, we conduct 3D simultaneous multicolor high-resolution live imaging to demonstrate in vivo that newly synthesized glycosylphosphatidylinositol-anchored proteins having a very long chain ceramide lipid moiety are clustered and sorted into specialized endoplasmic reticulum exit sites that are distinct from those used by transmembrane proteins. Furthermore, we show that the chain length of ceramide in the endoplasmic reticulum membrane is critical for this sorting selectivity. Our study provides the first direct in vivo evidence for lipid chain length–based protein cargo sorting into selective export sites of the secretory pathway.

scholarly journals Identification and Characterization of a Peptidoglycan Hydrolase, MurA, of Listeria monocytogenes, a Muramidase Needed for Cell Separation

2003 ◽  
Vol 185 (23) ◽  
pp. 6801-6808 ◽  
Author(s):  
Shannon A. Carroll ◽  
Torsten Hain ◽  
Ulrike Technow ◽  
Ayub Darji ◽  
Philippos Pashalidis ◽  
...  
Keyword(s):  
Cell Wall ◽  
Listeria Monocytogenes ◽  
Cell Separation ◽  
Bacterial Species ◽  
Surface Protein ◽  
Wild Type ◽  
Terminal Domain ◽  
Cell Wall Hydrolase ◽  
Characteristic Features ◽  
Type Gene

ABSTRACT A novel cell wall hydrolase encoded by the murA gene of Listeria monocytogenes is reported here. Mature MurA is a 66-kDa cell surface protein that is recognized by the well-characterized L. monocytogenes-specific monoclonal antibody EM-7G1. MurA displays two characteristic features: (i) an N-terminal domain with homology to muramidases from several gram-positive bacterial species and (ii) four copies of a cell wall-anchoring LysM repeat motif present within its C-terminal domain. Purified recombinant MurA produced in Escherichia coli was confirmed to be an authentic cell wall hydrolase with lytic properties toward cell wall preparations of Micrococcus lysodeikticus. An isogenic mutant with a deletion of murA that lacked the 66-kDa cell wall hydrolase grew as long chains during exponential growth. Complementation of the mutant strain by chromosomal reintegration of the wild-type gene restored expression of this murein hydrolase activity and cell separation levels to those of the wild-type strain. Studies reported herein suggest that the MurA protein is involved in generalized autolysis of L. monocytogenes.

Feasting Ritually: An Ethnography on the Implications of Feasts in Religious Rituals

2021 ◽  
pp. 0972558X2110571
Author(s):  
Anil Gopi
Keyword(s):  
Social Life ◽  
The Other ◽  
Social Solidarity ◽  
Cultural Significance ◽  
Religious Rituals ◽  
The People ◽  
Religious Festivals ◽  
The World ◽  
Characteristic Features ◽  
And Gender

Food and feast are integral and key components of human cultures across the world. Feasts associated with religious rituals have special social and cultural significance when compared to those in any other festivities or celebrations in people’s life. In this study, an approach is made to comparatively analyze the feasts at religious festivals of two distinctive groups of people, one with a characteristic of simple society and the other of a complex society. The annual feast happening at the hamlets of the Anchunadu Vellalar community in the last days of the calendar year is an occasion that portrays the egalitarian nature of the people. While this feast is restricted within a single community of particular caste affiliation and geographical limitations, the feast associated with the kaliyattam ritual of village goddess in North Malabar is much wider in scope and participation. The enormous feast brings the people in a larger area and exhibits a solidarity that cuts across boundaries of religion, caste and community. Beyond the factors of social solidarity and togetherness, these events also illustrate its divisive characters mainly in terms of social hierarchy and gender. A comparative study of both the two feasts of two different contexts reveals the characteristic features of religious feasts and the value of food and feast in social life and solidarity and also how it acts as a survival of their past and as a tradition.

scholarly journals Limited ER quality control for GPI-anchored proteins

2016 ◽  
Vol 213 (6) ◽  
pp. 693-704 ◽  
Author(s):  
Natalia Sikorska ◽  
Leticia Lemus ◽  
Auxiliadora Aguilera-Romero ◽  
Javier Manzano-Lopez ◽  
Howard Riezman ◽  
...  
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Misfolded Proteins ◽  
Control Mechanisms ◽  
Gpi Anchor ◽  
Er Quality Control ◽  
Entire Class ◽  
Er Export ◽  
Export Signal

Endoplasmic reticulum (ER) quality control mechanisms target terminally misfolded proteins for ER-associated degradation (ERAD). Misfolded glycophosphatidylinositol-anchored proteins (GPI-APs) are, however, generally poor ERAD substrates and are targeted mainly to the vacuole/lysosome for degradation, leading to predictions that a GPI anchor sterically obstructs ERAD. Here we analyzed the degradation of the misfolded GPI-AP Gas1* in yeast. We could efficiently route Gas1* to Hrd1-dependent ERAD and provide evidence that it contains a GPI anchor, ruling out that a GPI anchor obstructs ERAD. Instead, we show that the normally decreased susceptibility of Gas1* to ERAD is caused by canonical remodeling of its GPI anchor, which occurs in all GPI-APs and provides a protein-independent ER export signal. Thus, GPI anchor remodeling is independent of protein folding and leads to efficient ER export of even misfolded species. Our data imply that ER quality control is limited for the entire class of GPI-APs, many of them being clinically relevant.

scholarly journals The Traumatic Syndrome

1972 ◽  
Vol 17 (5) ◽  
pp. 391-396 ◽  
Author(s):  
Hector Warnes
Keyword(s):  
Life Style ◽  
Traumatic Event ◽  
The Other ◽  
Concentration Camp ◽  
Dynamic Pattern ◽  
Traumatic Neurosis ◽  
Concentration Camp Survivors ◽  
Characteristic Features

This paper demonstrates both the similarities and the differences between concentration camp survivors and those suffering from other forms of psychiatric reactions resulting from trauma. In the former the systematic degradation, humiliation and persecution over a prolonged period of time, along with a sense of hopelessness and/or helplessness are characteristic features. Found at the other extreme of the spectrum is the acute traumatic event occurring in civil life and resulting in a classical traumatic neurosis but not leading to a total transformation of personality and life style. Between these two forms of psychiatric reactions there are various pathogenetic and pathoplastic mechanisms, sometimes overlapping but showing the underlying dynamic pattern of survival threat.

Sign in / Sign up

Export Citation Format

Share Document