Vesicle membrane associated transporters

Studies with diatoms have revealed that silicic acid is pumped from the surrounding marine or freshwater environment into the cell against a concentration gradient through specific, outer membrane-associated transporters that were revealed recently by Hildebrand, Volcani and their colleagues14. Transporters related to those in the outer membrane may also facilitate entry into the membrane-enclosed silica deposition vesicle within the cell15. 

A few substances are so large or impermeant that they can enter cells only by endocytosis, the process by which the substance is bound at a cell-surface receptor, engulfed by the cell membrane, and carried into the cell by pinching off of the newly formed vesicle inside the membrane. The substance can then be released inside the cytosol by breakdown of the vesicle membrane. Figure 1-5D. This process is responsible for the transport of vitamin B12, complexed with a binding protein (intrinsic factor) across the wall of the gut into the blood. Similarly, iron is transported into hemoglobin-synthesizing red blood cell precursors in association with the protein transferrin. Specific receptors for the transport proteins must be present for this process to work. 

Schematic illustration of a generalized cholinergic junction (not to scale). Choline is transported into the presynaptic nerve terminal by a sodium-dependent choline transporter (CHT). This transporter can be inhibited by hemicholinium drugs. In the cytoplasm, acetylcholine is synthesized from choline and acetyl -A (AcCoA) by the enzyme choline acetyltransferase (ChAT). Acetylcholine is then transported into the storage vesicle by a second carrier, the vesicle-associated transporter (VAT), which can be inhibited by vesamicol. Peptides (P), adenosine triphosphate (ATP), and proteoglycan are also stored in the vesicle. Release of transmitter occurs when voltage-sensitive calcium channels in the terminal membrane are opened, allowing an influx of calcium. The resulting increase in intracellular calcium causes fusion of vesicles with the surface membrane and exocytotic expulsion of acetylcholine and cotransmitters into the junctional cleft (see text). This step can he blocked by botulinum toxin. Acetylcholine s action is terminated by metabolism by the enzyme acetylcholinesterase. Receptors on the presynaptic nerve ending modulate transmitter release. SNAPs, synaptosome-associated proteins VAMPs, vesicle-associated membrane proteins.

FIGURE 23.7 Dopamine (DA) is synthesized within neuronal terminals from the precursor tyrosine by the sequential actions of the enzymes tyrosine hydroxylase, producing the intermediary L-dihydroxyphenylalanine (Dopa), and aromatic L-amino acid decarboxylase. In the terminal, dopamine is transported into storage vesicles by a transporter protein (T) associated with the vesicular membrane. Release, triggered by depolarization and entry of Ca2+, allows dopamine to act on postsynaptic dopamine receptors (DAR). Several distinct types of dopamine receptors are present in the brain, and the differential actions of dopamine on postsynaptic targets bearing different types of dopamine receptors have important implications for the function of neural circuits. The actions of dopamine are terminated by the sequential actions of the enzymes catechol-O-methyl-transferase (COMT) and monoamine oxidase (MAO), or by reuptake of dopamine into the terminal. 

With the isolated perfused duodenum, there is a rapid increase in calcium transport in response to the addition of calcitriol to the perfusion medium. Isolated enterocytes and osteoblasts also show a rapid increase in calcium uptake in response to calcitriol. It is not associated with changes in mRNA or protein synthesis, but seems to be because of recruitment of membrane calcium transport proteins from intracellular vesicles to the cell surface. It is inhibited by the antimicrotubule compound colchicine. It can only be demonstrated in tissues from animals that are adequately supplied with vitamin D in vitamin D-deficient animals, the increase in intestinal calcium absorption occurs only more slowly, together with the induction of calbindin. 

Fig. 5. Proposed mechanism of ATP synthesis coupled to methyl-coenzyme M (CH3-S-C0M) reduction to CH4 The reduction of the heterodisulfide (CoM-S-S-HTP) as a site for primary translocation. ATP is synthesized via membrane-bound -translocating ATP synthase. CoM-S-S-HTP, heterodisulfide of coenzyme M (H-S-CoM) and 7-mercaptoheptanoylthreonine phosphate (H-S-HTP) numbers in circles, membrane-associated enzymes (1) CH3-S-C0M reductase (2) dehydrogenase (3) heterodisulfide reductase 2[H] can be either H2, reduced coenzymeF420 F420H2) or carbon monoxide the hatched box indicates an electron transport chain catalyzing primary translocation the stoichiometry of translocation (2H /2e , determined in everted vesicles) was taken from ref. [117] z is the unknown If /ATP stoichiometry A/iH, transmembrane electrochemical...

A FIGURE 18-1 Overview of synthesis of major membrane lipids and their movement into and out of cells. Membrane lipids (e.g., phospholipids, cholesterol) are synthesized through complex multienzyme pathways that begin with sets of water-soluble enzymes and intermediates in the cytosol (D) that are then converted by membrane-associated enzymes into water-insoluble products embedded in the membrane (B), usually at the interface between the cytosolic leaflet of the endoplasmic reticulum (ER) and the cytosol. Membrane lipids can move from the ER to other organelles (H), such as the Golgi apparatus or the mitochondrion, by either vesicle-mediated or other poorly defined mechanisms. Lipids can move into or out of cells by plasma-membrane transport proteins or by lipoproteins. Transport proteins similar to those described in Chapter 7 that move lipids (0) include sodium-coupled symporters that mediate import CD36 and SR-BI superfamily proteins that can mediate... 

Thioacylation frequently dictates plasma membrane targeting of proteins lacking trans-membrane spans. In the case of p59 5 " targeting occurs directly, with the iV-myristoylated protein becoming thioacylated and plasma membrane associated rapidly upon completion of synthesis. In contrast, p56 appears to be thioacylated on intracellular membranes and arrive at the plasma membrane via vesicular transport (bound to the cytoplasmic face of secretory vesicles) (M. Bijlmakers, 1999). In yet another targeting variation, newly synthesized A-myristoylated G, a dually acylated trimeric G protein cx-subunit, associates with all cellular membranes but accumulates eventually at the plasma membrane the plasma membrane form is the only one that is both A-myristoylated and thioacylated. 

Microtubules, cyhndrical tubes composed of tubulin subunits, are present in all nucleated cells and the platelets in blood (Fig. 10.26). They are responsible for the positioning of organelles in the cell cytoplasm and the movement of vesicles, including phagocytic vesicles, exocytotic vesicles, and the transport vesicles between the ER, Golgi, and endosomes (see Fig. 10.24). They also form the spindle apparatus for cell division. The microtnbnle network (the minus end) begins in the nucleus at the centriole and extends outward to the plasma membrane (usually the plus end). Microtubule-associated proteins (MAPs) attach microtubules to other cellular components, and can determine cell shape and polarity. 

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