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It is composed mostly of cellulose and gives the plant cell support.

This type of structural organization of nucleolus is found in eukaryotic cells.

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Start studying Cells/Organelles/Photosynthesis

Photosynthesis takes place inside plant cells in small things called chloroplasts. Chloroplasts (mostly found in the mesophyll layer) contain a green substance called chlorophyll. Below are the other parts of the cell that work with the chloroplast to make photosynthesis happen.


Leaves also use veins to export sugar to roots and other nonphotosynthetic parts of the plant.

It serves as a physical barrier, and allows only specific molecules to pass into the cell.

Cytoplasm is a gel-like structure that holds together all the internal structures of a cell.

How is sugar made by photosynthesis in a plant cell ..

In a way, the converse of the centriole in the animal cell is the chloroplast in the plant cell.

The similarities between RME-1 and dynamin-family pinchases were extended by the discovery that RME-1 binds to N-BAR protein amphiphysin/AMPH-1 (). Amphiphysin was originally discovered as a binding partner of mammalian neuron-specific dynamin I (). The interaction between RME-1 and AMPH-1 was discovered by focusing on the C-terminal, Eps15-homology (EH) of RME-1. EH-domains generally target Asn-Pro-Phe (NPF) motifs in binding partners, and the RME-1/EHD-family subfamily of EH-domains displays a preference for acidic residues after the NPF target sequence (). AMPH-1 has two central NPF(D/E) containing sequences, and RNAi or deletion displaced RME-1 from recycling endosome to the cytoplasm in the adult intestine. AMPH-1 colocalized with RME-1 on basolateral recycling endosomes of the intestine, and mutants were defective in recycling cargo proteins hTfR and hTAC. The binding of RME-1 to AMPH-1 was shown to be mediated by the EH/NPF interaction, and AMPH-1 expressed from an intestine-specific promoter could rescue the hTfR recycling defect, but not if the NPF sequences were mutated to NPA. Taken together these results indicated that RME-1 and AMPH-1 function together on recycling endosomes to return recycling receptors to the basolateral cell surface.

Figure 6. RME-1 is a membrane bending protein required for recycling endosome function. (A) Shows the basal surface of the intestinal cells in animal expressing GFP::RME-1. Note that the tubulovesicular network of basolateral recycling endosomes is labeled by GFP::RME-1. (B) Shows an immuno-EM image of fixed intestinal tissue using an anti-RME-1 antibody. Endogenous RME-1 is restricted to the junction of the vesicular and tubular regions of the recycling endosomes where it is likely to regulate fission of cargo-containing tubules. (C) Purified RME-1 proteins were reconstituted on synthetic liposomes. In the presence of ATPγS, RME-1 assembles in rings (striations on tubules) and squeezes the liposome membranes into narrow tubules in a manner very similar to that of Dynamin (GTPγS).

All plants are made up of one or more units called cells

Resulting small bubbles of food inside the cell fuse with digestive organelles called lysosomes.

RAB-10 is a key basolateral recycling regulator in the intestine (; ; ). mutants display obvious vacuoles in the intestine, some large enough to observe at the dissecting-microscope level (). These vacuoles were identified as basolateral endosomes because they accumulate fluid-phase endocytic markers from the body cavity, including GFP secreted from muscle cells and fluorescent BSA microinjected into the body cavity. Furthermore these vacuoles label for endosome markers RAB-5 and ARF-6, and accumulate high levels of the ARF-6-dependent recycling cargo hTAC::GFP (; ). Normal-sized RAB-5-positive early endosomes also accumulate in the mutant intestine (). Furthermore the number of RME-1-positive basolateral recycling endosomes is greatly reduced, and those that remain lose their normal tubular morphology, now appearing punctate. RAB-10 partially colocalizes with the early endosome marker RAB-5, and often appears adjacent to RME-1-labeled tubular recycling endosomes. These RAB-10 positive endosomes may be the equivalent of common recycling endosomes (CREs) that are the primary location of Rab10 in polarized MDCK cells (). The CRE is a recycling compartment that receives and sorts cargo from basolateral and apical membranes, and is thus a specialized organelle of polarized epithelia (). The results in suggested that RAB-10 functions at the junction of early endosome to recycling endosome transport. mutants do not appear to affect Golgi, late endosomes, or apical recycling endosomes, suggesting a specific role in this transport step (). Rab10 appears to be specific for basolateral traffic in mammalian MDCK cells as well ().

RAB-10 function in initially appeared limited to polarized cells. In addition to its role in the intestine, RAB-10 functions in the recycling of the postsynaptic recycling receptor GLR-1, and in the secretion of neuropeptides in neurons (polarized cells), but did not obviously affect endocytosis in non-polarized coelomocytes or oocytes (; ; ). This was surprising since RAB-10 is ubiquitously expressed. In fact, further analysis revealed that RAB-10 does play a role in membrane traffic in non-polarized cells, but this function is redundant with that of its closest paralog, RAB-8 (). While and single mutants are viable and fertile, many animals depleted of both RAB-10 and RAB-8 arrest as larvae, and the surviving adults are invariably sterile. The sterility appears to result from a block in germline secretion and/or recycling, with gonads depleted of both RAB-10 and RAB-8 trapping transmembrane protein SNB-1 in intracellular vesicles. The larval arrest phenotype may also result from defects in secretion and/or endocytic recycling in other cell types when RAB-10 and RAB-8 are missing. These results suggest that RAB GTPase redundancy can differ with cell type. It remains to be determined if the redundancy in non-polarized cells represents simple biochemical interchangeability of these Rabs, or reveals redundant recycling pathways that have distinct functions in polarized cells but overlapping roles in non-polarized cells.

All membranous eukaryotic cell organelles have the common feature of a phospholipid bilayer, although the proteins differ in each case.
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  • The organelles are only found in plant cells ..

    It must produce a working copy of that information, called RNA, which it ships out into the rest of the cell.

  • In plant cells, this cell organelle has an ..

    Many materials, including some proteins, are sorted by the functionally cellular membranes of the endomembrane system.

  • Plant cells take part in photosynthesis to ..

    Chloroplasts are organelles in plant and bacteria cells that contain the chlorophyll used in ..

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What's the difference between Cellular Respiration and Photosynthesis

The SNX-1 BAR domain binds to the C-terminal third of the DNA J-domain protein RME-8, originally identified in the yolk transport screens (; ). and mutants missort MIG-14 to lysosomes in the intestine, and display defective polarity of mechanosensory neurites, suggesting a defect in Wnt signaling (). Interestingly, the centrally located RME-8 J-domain binds to HSP-1/Hsc70, a protein folding chaperone (; ; ). SNX-1 and RME-8 colocalize to a subset of early endosomes that are often directly juxtaposed to Golgi ministacks (). This proximity may facilitate endosome to Golgi transport. J-domain proteins typically recruit and activate Hsc70 proteins, localizing their activity in the assembly and disassembly of protein complexes, such as clathrin lattices (; ). Thus current models propose that RME-8 acts on subdomains of endosomes enriched in retromer complexes, disassembling clathrin lattices that encroach from neighboring endosomal subdomains that are enriched in ESCRT complexes (). In mammalian cells the ESCRT-0 component HRS (HGRS-1) binds to a specialized flat clathrin lattice on endosomes that is thought to concentrate ESCRT complexes and degradative cargo (; ; ). Consistent with this model, mutants or RNAi of , , and mislocalize and degrade intestinally expressed MIG-14 via the lysosome, and over-accumulate endosomal clathrin (). These results suggest that endosomes maintain distinct recycling and degradative subdomains via molecular antagonism between recycling and degradative regulatory proteins. The requirement for RME-8 in retrograde recycling, and its binding and colocalization with Snx1 and other retromer components, is conserved in mammals (; ).

Where in a plant cell (what organelle) does photosynthesis occur?

SNX-3 homologs are known to play important roles in retrograde trafficking in yeast and mammals. The yeast SNX-3 homolog Grd19 is required for the retrograde trafficking of the iron transporter complex Fet3p-Ftr1p (). However, unlike (the homolog) mutants, mutants display only minor defects in Vps10p trafficking (; ). Additionally, Grd19p binds directly to the Fet3p-Ftr1p cargo, leading to models stating that Grd19p/Snx3 is a cargo specific adaptor promoting the inclusion of Fet3p-Ftr1p into Vps5p/Vps17p containing retromer tubules (). In mammals, Snx3 along with Vps35 affects transferrin receptor (Tfr) recycling in erythroid progenitor cells (). Whether Snx1 is involved in this process is not known.

List of Cell Organelles & Their Functions | Sciencing

By forming a concentration gradient, Wnt ligands provide positional information to cells in an organism, particularly anterior-posterior polarized cell divisions, cell migrations, and axon pathfinding (see WormBook chapter ). Wnt-producing cells secrete Wnt ligands using the MIG-14 transmembrane chaperone, which binds to nascent Wnt ligands such as EGL-20 in the Golgi. MIG-14 then chaperones Wnt ligands to the plasma membrane for release (; ). For subsequent rounds of Wnt secretion, MIG-14 must be endocytosed in a clathrin/AP2-dependent manner, and MIG-14 must be recycled to the Golgi via retrograde transport (; ). Blocking the endocytosis of MIG-14 blocks its function and greatly impairs Wnt secretion, resulting in Wnt phenotypes. MIG-14/Wntless endocytosis and recycling is a conserved process that has been directly demonstrated in , , and mammalian cells (; ). In the absence of retromer components VPS-35, VPS-26, or SNX-3, MIG-14 is missorted to lysosomes after endocytosis and is degraded, resulting in low cellular levels of MIG-14 and poor secretion of Wnt ligands such as EGL-20 (; ). This produces severe defects in Wnt signaling, including defective migration of Q-cell descendants and defective polarity of mechanosensory neurites (; ; ; ). While defects in retrograde recycling of MIG-14 result in Wnt signaling defects, any trafficking defect that inhibits MIG-14 from reaching the Golgi, or trafficking defects of Wnt receptors, can affect Wnt signaling (; ). Hence, only a subset of trafficking mutants that produce Wnt phenotypes affect retrograde endosome-to-Golgi traffic.

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