Uptake of endocytic markers by rice cells: variations related to the growth phase

Bahaji, Abdellatif; Cornejo, M. J.; Ortiz-Zapater, Elena; Contreras, Inmaculada; Aniento, Fernando

doi:10.1078/0171-9335-00146

Cited by 15 publications

(13 citation statements)

References 28 publications

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“…When this literature is critically examined, the data conflict. In one study using biotin-labeled BSA (LBSA), the uptake of the BSA was drastically decreased in rice cells when they were in the exponential phase of growth (Bahaji et al, 2001). In soybean cell cultures, however, the results were opposite to those using rice cells (Horn et al, 1992).…”

Section: Endocytosis Of Scamentioning

confidence: 82%

“…One difficulty with using biotin, though, as reported, is that any protein labeled with biotin is endocytosed. Insulin, RNase, and bovine serum albumin (BSA) have been used to study endocytosis in cultured soybean (Glycine max) and rice cells (Horn et al, 1990(Horn et al, , 1992Bahaji et al, 2001). In these studies, the proposal was that receptor-mediated endocytosis occurred in plant cells via biotin receptors located on the plasma membrane.…”

Section: Endocytosis Of Scamentioning

confidence: 99%

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Exogenous Free Ubiquitin Enhances Lily Pollen Tube Adhesion to an in Vitro Stylar Matrix and May Facilitate Endocytosis of SCA

et al. 2006

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Pollen tube adhesion and guidance on extracellular matrices within the pistil are essential processes that convey the pollen tube cell and the sperm cells to the ovule. In this study, we purified an additional molecule from the pistil that enhances pollen tube adhesion when combined with the SCA (stigma/stylar cysteine-rich adhesin)/pectin matrix in our in vitro assay. The enhancer of adhesion was identified as free ubiquitin (Ub). This was confirmed by use of bovine Ub as a substitute for lily (Lilium longiflorum Thunb.) stigma Ub. To study the interaction of SCA and Ub with the lily pollen tube, we labeled both proteins with biotin. We observed uptake of biotin-labeled SCA and Ub into the pollen tube cells in vitro using confocal microscopy. For SCA, a strong signal occurred first at the tip of the pollen tube, suggestive of an endocytosis event, and then progressively throughout the tube cytoplasm. SCA was also localized inside the in vivo pollen tube using immunogold electron microscopy and found to be present in endosomes, multivesicular bodies, and vacuoles, all known to be endocytic compartments. It was also confirmed that SCA is endocytosed in the in vitro adhesion assay. Internalization of SCA was increased in pollen tubes treated with exogenous Ub compared to those without Ub, suggesting that Ub may facilitate SCA endocytosis. These results show that Ub can act as an enhancer of pollen tube adhesion in vitro and that it is taken up into the pollen tube as is SCA. The Ub machinery may play a role in pollen tube adhesion and guidance in lily.

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Section: Endocytosis Of Scamentioning

confidence: 82%

Section: Endocytosis Of Scamentioning

confidence: 99%

Exogenous Free Ubiquitin Enhances Lily Pollen Tube Adhesion to an in Vitro Stylar Matrix and May Facilitate Endocytosis of SCA

et al. 2006

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“…Recently, a biochemical marker for receptor-mediated endocytosis was developed for rice suspension cells based on the specific binding and internalization of biotin-labeled proteins (Bahaji et al, 2001). FM1-43 has some advantages over protein markers in that it is a membrane marker whose uptake can be both imaged and easily quantified in living intact cells.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, FM1-43 has a positive electric charge that prevents it from crossing the membrane, so it remains partitioned in the outer lipid leaflet of the animal cell plasma membrane (Sulzer and Holtzman, 1989;Schote and Seelig, 1998). Thus, we speculate that FM1-43 does not enter plant cells via the nonendocytic pathway observed for the phosphatidylcholine analog (Grabski et al, 1993) but serves as a marker for temperature-dependent membrane internalization from the plasma membrane via vesicle traffic, as is well established for FM4-64 in yeast (Vida and Emr, 1995).Recently, a biochemical marker for receptor-mediated endocytosis was developed for rice suspension cells based on the specific binding and internalization of biotin-labeled proteins (Bahaji et al, 2001). FM1-43 has some advantages over protein markers in that it is a membrane marker whose uptake can be both imaged and easily quantified in living intact cells.…”

mentioning

confidence: 99%

Uptake of a Fluorescent Marker in Plant Cells Is Sensitive to Brefeldin A and Wortmannin

2002

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We assessed FM1-43 [ N -(3-triethylammoniumpropyl)-4-(4-[dibutylamino]styryl)pyridinium dibromide] as a fluorescent endocytosis marker in intact, walled plant cells. At 4 ؇ C, FM1-43 stained the plasma membrane, and after 30 to 120 min of incubation at 26 ؇ C, FM1-43 labeled cytoplasmic vesicles and then the vacuole. Fluorimetric quantitation demonstrated dye uptake temperature sensitivity ( ‫ف‬ 65% reduction at 16 ؇ C, Ͼ 90% at 4 ؇ C). FM1-43 uptake in suspension cells was stimulated more than twofold by brefeldin A and inhibited ‫ف‬ 0.4-fold by wortmannin. FM1-43 delivery to the vacuole was largely inhibited by brefeldin A, although overall uptake was stimulated, and brefeldin A treatment caused the accumulation of large prevacuolar endosomal vesicles heavily labeled with FM1-43. Three-dimensional time lapse imaging revealed that FM1-43-labeled vacuoles and vesicles are highly dynamic. Thus, FM1-43 serves as a fluorescent marker for imaging and quantifying membrane endocytosis in intact plant cells. INTRODUCTIONEndocytosis in animal cells begins with the budding of invaginated coated pits from the plasma membrane into coated vesicles, which then uncoat and fuse with the endocytic organelles (Gruenberg et al., 1989;Gruenberg and Maxfield, 1995). By this action, both membrane proteins and fluid phase molecules are sequestered from the cell exterior into intracellular organelles, from where they can recycle to the plasma membrane or be transported to other destinations, such as the lysosomes. Thus, endocytosis serves to balance membrane secretion and to remove, transport, or degrade receptor ligand complexes from the cell surface (Goldstein et al., 1985). Although clathrin coatdependent endocytosis is involved in receptor internalization, clathrin-independent endocytosis pathways also contribute to internalization. These include uptake via nonclathrin-coated caveolae (Anderson, 1998), macropinocytosis (Swanson, 1989;Hewlett et al., 1994), and phagocytosis (Aderem and Underhill, 1999).Our understanding of animal cell endocytosis was advanced by the use of fluorescent and electron-opaque markers that can be internalized Maxfield, 1988, 1989;Griffiths et al., 1989). The use of fluid phase markers has permitted the development of assays that reconstitute endocytic vesicle fusion (Braell, 1987(Braell, , 1992Gruenberg et al., 1989;Emans et al., 1995;Emans and Verkman, 1996) and led to the identification of many proteins that catalyze and control fusion, such as the small GTPase rab5 (Gorvel et al., 1991) and its effector proteins (Christoforidis et al., 1999a(Christoforidis et al., , 1999bMcBride et al., 1999).In plants, there is evidence that endocytosis is likely to occur (Low and Chandra, 1994; for review, see Battey et al., 1999;Marcote et al., 2000). Endocytosis is postulated to counterbalance membrane secretion (Samuels and Bialputra, 1990) and permit cell volume to respond to changes in osmolality (Thiel et al., 1998;Kubitscheck et al., 2000). However, the study of plant cell endocytosis has been hampered by t...

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“…However, numerous subsequent reports that used endocytic markers (for review, see Low and Chandra, 1994;Bahaji et al, 2001;Battey et al, 1999), as well as a number of recent localization and functional studies employing membrane-associated styryl FM dyes, filipin-labeled plant sterols, the fluid-phase marker Lucifer Yellow, green fluorescent protein (GFP)/yellow fluorescent protein (YFP)-tagged Rab GTPases, and BP-80 (a prevacuolar compartment/ multivesicular body marker) and the fungal inhibitor of vesicular traffic, brefeldin A (BFA), clarified the existence and extraordinary dynamics of endocytic activity in plant cells (Geldner et al, 2001(Geldner et al, , 2003Ueda et al, 2001;Baluška et al, 2002Baluška et al, , 2004Emans et al, 2002;Inaba et al, 2002;Grebe et al, 2003;Tse et al, 2004).…”

Section: Endocytosis In Plantsmentioning

confidence: 99%

Endocytosis, Actin Cytoskeleton, and Signaling

et al. 2004

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Uptake of endocytic markers by rice cells: variations related to the growth phase

Cited by 15 publications

References 28 publications

Exogenous Free Ubiquitin Enhances Lily Pollen Tube Adhesion to an in Vitro Stylar Matrix and May Facilitate Endocytosis of SCA

Exogenous Free Ubiquitin Enhances Lily Pollen Tube Adhesion to an in Vitro Stylar Matrix and May Facilitate Endocytosis of SCA

Uptake of a Fluorescent Marker in Plant Cells Is Sensitive to Brefeldin A and Wortmannin

Endocytosis, Actin Cytoskeleton, and Signaling

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