Berkeley body

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Berkeley bodies are organelles unique to the yeast cell Saccharomyces cerevisiae , with a secretory mutation in the genes sec7 and sec14. The function of the organelle lies in the CTV (cytoplasm to vacuole targeting) pathway, which is a transport pathway for certain vacuolar hydrolases to be degenerated. The Berkeley body acts as the transport medium from the cytoplasm to the vacuole within this pathway. Studies have shown that Berkeley bodies share structural similarities with autophagosomes, which are involved in autophagy. [1]

The organelle consists of two enclosed membranes forming an enclosed lumen, which contains cytoplasm. It is formed by vesicles budding off the Golgi apparatus or the endoplasmic reticulum. They were discovered in 1980 by Peter Novick and Randy Schekman, of the Department of Biochemistry, University of California, Berkeley. [2]

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Endomembrane system Membranes in the cytoplasm of a eukaryotic cell

The endomembrane system is composed of the different membranes that are suspended in the cytoplasm within a eukaryotic cell. These membranes divide the cell into functional and structural compartments, or organelles. In eukaryotes the organelles of the endomembrane system include: the nuclear membrane, the endoplasmic reticulum, the Golgi apparatus, lysosomes, vesicles, endosomes, and plasma (cell) membrane among others. The system is defined more accurately as the set of membranes that form a single functional and developmental unit, either being connected directly, or exchanging material through vesicle transport. Importantly, the endomembrane system does not include the membranes of plastids or mitochondria, but might have evolved partially and from the actions of the latter.

Golgi apparatus Cell organelle that packages proteins for export

The Golgi apparatus, also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. Part of the endomembrane system in the cytoplasm, it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus.

Vacuole Membrane-bound organelle in cells containing fluid

A vacuole is a membrane-bound organelle which is present in plant and fungal cells and some protist, animal, and bacterial cells. Vacuoles are essentially enclosed compartments which are filled with water containing inorganic and organic molecules including enzymes in solution, though in certain cases they may contain solids which have been engulfed. Vacuoles are formed by the fusion of multiple membrane vesicles and are effectively just larger forms of these. The organelle has no basic shape or size; its structure varies according to the requirements of the cell.

Vesicle (biology and chemistry) Any small, fluid-filled, spherical organelle enclosed by a membrane

In cell biology, a vesicle is a structure within or outside a cell, consisting of liquid or cytoplasm enclosed by a lipid bilayer. Vesicles form naturally during the processes of secretion (exocytosis), uptake (endocytosis) and transport of materials within the plasma membrane. Alternatively, they may be prepared artificially, in which case they are called liposomes. If there is only one phospholipid bilayer, they are called unilamellar liposome vesicles; otherwise they are called multilamellar. The membrane enclosing the vesicle is also a lamellar phase, similar to that of the plasma membrane, and intracellular vesicles can fuse with the plasma membrane to release their contents outside the cell. Vesicles can also fuse with other organelles within the cell. A vesicle released from the cell is known as an extracellular vesicle.

Secretion is the movement of material from one point to another, such as a secreted chemical substance from a cell or gland. In contrast, excretion is the removal of certain substances or waste products from a cell or organism. The classical mechanism of cell secretion is via secretory portals at the plasma membrane called porosomes. Porosomes are permanent cup-shaped lipoprotein structures embedded in the cell membrane, where secretory vesicles transiently dock and fuse to release intra-vesicular contents from the cell.

Autophagy Cellular catabolic process in which cells digest parts of their own cytoplasm

Autophagy is the natural, conserved degradation of the cell that removes unnecessary or dysfunctional components through a lysosome-dependent regulated mechanism. It allows the orderly degradation and recycling of cellular components. Although initially characterized as a primordial degradation pathway induced to protect against starvation, it has become increasingly clear that autophagy also plays a major role in the homeostasis of non-starved cells. Defects in autophagy have been linked to various human diseases, including neurodegeneration and cancer, and interest in modulating autophagy as a potential treatment for these diseases has grown rapidly.

Randy Schekman American cell biologist

Randy Wayne Schekman is an American cell biologist at the University of California, Berkeley, former editor-in-chief of Proceedings of the National Academy of Sciences and former editor of Annual Review of Cell and Developmental Biology. In 2011, he was announced as the editor of eLife, a new high-profile open-access journal published by the Howard Hughes Medical Institute, the Max Planck Society and the Wellcome Trust launching in 2012. He was elected to the National Academy of Sciences in 1992. Schekman shared the 2013 Nobel Prize for Physiology or Medicine with James Rothman and Thomas C. Südhof for their ground-breaking work on cell membrane vesicle trafficking.

Phagosome

In cell biology, a phagosome is a vesicle formed around a particle engulfed by a phagocyte via phagocytosis. Professional phagocytes include macrophages, neutrophils, and dendritic cells (DCs).

Endoplasm Also known as entoplasm

Endoplasm generally refers to the inner, dense part of a cell's cytoplasm. This is opposed to the ectoplasm which is the outer (non-granulated) layer of the cytoplasm, which is typically watery and immediately adjacent to the plasma membrane. These two terms are mainly used to describe the cytoplasm of the amoeba, a protozoan, eukaryotic cell. The nucleus is separated from the endoplasm by the nuclear envelope. The different makeups/viscosities of the endoplasm and ectoplasm contribute to the amoeba's locomotion through the formation of a pseudopod. However, other types of cells have cytoplasm divided into endo- and ectoplasm. The endoplasm, along with its granules, contains water, nucleic acids, amino acids, carbohydrates, inorganic ions, lipids, enzymes, and other molecular compounds. It is the site of most cellular processes as it houses the organelles that make up the endomembrane system, as well as those that stand alone. The endoplasm is necessary for most metabolic activities, including cell division.

Cell physiology is the biological study of the activities that take place in a cell to keep it alive. The term physiology refers to normal functions in a living organism. Animal cells, plant cells and microorganism cells show similarities in their functions even though they vary in structure.

Outline of cell biology Overview of and topical guide to cell biology

The following outline is provided as an overview of and topical guide to cell biology:

ATG8

Autophagy-related protein 8 (Atg8) is a ubiquitin-like protein required for the formation of autophagosomal membranes. The transient conjugation of Atg8 to the autophagosomal membrane through a ubiquitin-like conjugation system is essential for autophagy in eukaryotes. Even though there are homologues in animals, this article mainly focuses on its role in lower eukaryotes such as Saccharomyces cerevisiae.

AuTophaGy related 1 (Atg1) is a 101.7kDa serine/threonine kinase in S.cerevisiae, encoded by the gene ATG1. It is essential for the initial building of the autophagosome and Cvt vesicles. In a non-kinase role it is - through complex formation with Atg13 and Atg17 - directly controlled by the TOR kinase, a sensor for nutrient availability.

Sec14

Sec14 is a cytosolic protein found in yeast which plays a role in the regulation of several cellular functions, specifically those related to intracellular transport. Encoded by the Sec14 gene, Sec14p may transport phosphatidylinositol and phosphatidylcholine produced in the endoplasmic reticulum and the Golgi body to other cellular membranes. Additionally, Sec14p potentially plays a role in the localization of lipid raft proteins. Sec14p is an essential gene in yeast, and is homologous in function to phosphatidylinositol transfer protein in mammals. A conditional mutant with non-functional Sec14p presents with Berkeley bodies and deficiencies in protein secretion.

An autophagosome is a spherical structure with double layer membranes. It is the key structure in macroautophagy, the intracellular degradation system for cytoplasmic contents. After formation, autophagosomes deliver cytoplasmic components to the lysosomes. The outer membrane of an autophagosome fuses with a lysosome to form an autolysosome. The lysosome's hydrolases degrade the autophagosome-delivered contents and its inner membrane.

Rab GTPases are molecular switches that regulate membrane traffic. They are active in their GTP-bound form and inactive when bound to GDP. The GTPase YPT1, and its mammalian homologue Rab1, regulate membrane-tethering events on three different pathways: autophagy, ER-Golgi, and intra-Golgi traffic. In the yeast Saccharomyces cerevisiae, many of the ATG proteins needed for macroautophagy are shared with the biosynthetic cytoplasm to the vacuole-targeting (CVT) pathway that transports certain hydrolases into the vacuole. Both pathways require YPT1; however, only the macroautophagy pathway is conserved in higher eukaryotes. In the macroautophagy pathway, Rab1 mediates the recruitment of Atg1 to the PAS. Rab1 regulates macroautophagy by recruiting its effector, Atg1, to the PAS to tether Atg9 vesicles to each other or to other membranes.

Intracellular transport Directed movement of vesicles and substances within a cell

Intracellular transport is the movement of vesicles and substances within a cell. Intracellular transport is required for maintaining homeostasis within the cell by responding to physiological signals. Proteins synthesized in the cytosol are distributed to their respective organelles, according to their specific amino acid’s sorting sequence. Eukaryotic cells transport packets of components to particular intracellular locations by attaching them to molecular motors that haul them along microtubules and actin filaments. Since intracellular transport heavily relies on microtubules for movement, the components of the cytoskeleton play a vital role in trafficking vesicles between organelles and the plasma membrane by providing mechanical support. Through this pathway, it is possible to facilitate the movement of essential molecules such as membrane‐bounded vesicles and organelles, mRNA, and chromosomes.

Exomer is a heterotetrameric protein complex similar to COPI and other adaptins. It was first described in the yeast Saccharomyces cerevisiae. Exomer is a cargo adaptor important in transporting molecules from the Golgi apparatus toward the cell membrane. The vesicles it is found on are different from COPI vesicles in that they do not appear to have a "coat" or "scaffold" around them.

Peter Novick is an American scientist who holds the George Palade Endowed Chair in the Department of Cellular and Molecular Medicine at the University of California, San Diego. His research interests focus on the biology of cell membranes, particularly the secretory pathway and other aspects of membrane trafficking and intracellular transport.

Susan Ferro-Novick is an American scientist who is a Distinguished Professor of Cellular and Molecular Medicine at the University of California, San Diego. Her research interests focus on the biology of cell membranes and their responses to cell stress, particularly related to membrane trafficking in the secretory and autophagy pathways, as well as a quality control pathway known as ER-phagy in the endoplasmic reticulum.

References

  1. Fulvio Reggiori, Chao-Wen Wang, Usha Nair, Takahiro Shintani, Hagai Abeliovich, and Daniel J. Klionsky, Early Stages of the Secretory Pathway, but Not Endosomes, Are Required for Cvt Vesicle and Autophagosome Assembly in Saccharomyces cerevisiae, from Molecular Biology of the Cell Vol. 15, 2189–2204, May 2004.
  2. Peter Novick, Charles Field and Randy Schekman. Identification of 23 Complementation Groups Required for Post-translational Events in the Yeast Secretory Pathway. Cell, Vol. 21, 205–215, August, 1980.