Calreticulin and the Endoplasmic Reticulum in Plant Cell Biology

Mariani, Paola; Navazio, Lorella; Zuppini, Anna

doi:10.1007/978-1-4419-9258-1_10

Cited by 14 publications

(16 citation statements)

References 74 publications

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“…The protein shares the same molecular structure identiWed for its animal homologue and seems to have similar functional properties (see review by Mariani et al 2003). One of the most important roles of CRT is calcium-storing function in the ER of plant cells (Persson et al 2001;Wyatt et al 2002).…”

Section: Introductionmentioning

confidence: 94%

Calreticulin expression and localization in plant cells during pollen–pistil interactions

Lenartowska

Lenartowski

Smoliński

et al. 2009

Planta

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In this report, the distributions of calreticulin (CRT) and its transcripts in Haemanthus pollen, pollen tubes, and somatic cells of the hollow pistil were studied. Immunoblot analysis of protein extracts from mature anthers, dry and germinated pollen, growing pollen tubes, and unpollinated/pollinated pistils revealed a strong expression of CRT. Both in vitro and in situ studies confirmed the presence of CRT mRNA and protein in pollen/pollen tubes and somatic cells of the pistil transmitting tract. The co-localization of these molecules in ER of these cells suggests that the rough ER is a site of CRT translation. In the pistil, accumulation of the protein in pollen tubes, transmitting tract epidermis (tte), and micropylar cells of the ovule (mc) was correlated with the increased level of exchangeable calcium. Therefore, CRT as a Ca(2+)-binding/buffering protein, may be involved in mechanism of regulation calcium homeostasis in these cells. The functional role of the protein in pollen-pistil interactions, apart from its postulated function in cellular Ca(2+) homeostasis, is discussed.

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Section: Introductionmentioning

confidence: 94%

Calreticulin expression and localization in plant cells during pollen–pistil interactions

Lenartowska

Lenartowski

Smoliński

et al. 2009

Planta

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“…One of the more abundant and highly conserved reticuloplasmins is calreticulin, which has been shown to play an important role in Ca 2+ binding (Michalak et al 1992) and may function in Ca 2+ sequestration and Ca 2+ -dependent protein folding (Michalak et al 1999). Calreticulin occurs ubiquitously in all eukaryotic organisms, and in the complex system of higher plants it is constitutively expressed in all meristematic and mature cell types (Mariani et al 2003). Its expression level appears to be related to the abundance of ER membranes.…”

Section: Introductionmentioning

confidence: 98%

“…Its expression level appears to be related to the abundance of ER membranes. As a molecular chaperone and Ca 2+ sensor within the ER, plant calreticulin shares a similar molecular structure and basic functions with its animal counterpart (Mariani et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Expression and localization of calreticulin in tobacco anthers and pollen tubes

Nardi

Feron

Navazio

et al. 2005

Planta

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The developmental expression pattern and localization of calreticulin were studied in Nicotiana tabacum L. anthers, pollen and pollen tubes. High transcript and protein levels were detected throughout anther development. Immunolocalization of calreticulin in the anthers showed particular dense label in tapetum and pollen at developmental stage 2, when the tapetum is highly active and the pollen tetrads are formed. Much lower transcript and protein levels were detected in dry and hydrated pollen and in pollen tubes. Immunofluorescence labeling of both chemically fixed and cryo-fixed and freeze-substituted pollen tubes showed the presence of calreticulin in Golgi apparatus and endoplasmic reticulum (ER). Calreticulin was seen throughout the stacks in the Golgi apparatus and in the areas with coated-Golgi vesicles but much less so in the ER. Calreticulin was not found in the secretory vesicles. A relatively intense label was occasionally seen adjacent to the wall of the tube. No significant label was observed in mitochondria, vacuoles, generative cells, cell wall or callose plugs. The present results are consistent with a role of calreticulin in Ca2+-dependent folding of secreted glycoproteins in tapetum, pollen and pollen tubes.

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“…Calreticulin also has other roles (Mariani et al 2003). As we mentioned above, the ER chaperone BiP is a very abundant protein, and at any given moment not all BiP molecules are involved in helping the folding of newly synthesized proteins.…”

Section: Glucosidases and Glucosyltransferase And The Calnexin/calrementioning

confidence: 99%

“…Finally, calreticulin is a calcium-binding protein and may be a key player in the regulation of calcium storage in the ER (Mariani et al 2003; see also Persson and Harper 2006, this volume). Calcium is certainly important for the action of ER folding helpers, because calcium ionophores are also UPR inducers, BiP is also a calcium-binding protein and calreticulin binds protein disulphide isomerase in a calcium-dependent process.…”

Section: Glucosidases and Glucosyltransferase And The Calnexin/calrementioning

confidence: 99%

The ER Folding Helpers: A Connection Between Protein Maturation, Stress Responses and Plant Development

Vitale

Denecke

2006

Plant Cell Monographs

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The main resident proteins of the endoplasmic reticulum (ER) collaborate to ensure that newly synthesized secretory proteins acquire their correct conformation. Most ER residents are therefore, directly or indirectly, folding helpers and controllers of the quality of newly synthesized secretory polypeptides. Genetic approaches have revealed that these helpers are necessary for virtually any major aspect of plant life, from differentiation to reproduction to interactions with the environment. Detailed biochemical analysis on the protein-protein interactions that occur during folding in the ER has been performed on a number of model secretory proteins, and the integration between genetics and biochemistry is a major future goal of this field of plant cell biology.

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Calreticulin and the Endoplasmic Reticulum in Plant Cell Biology

Cited by 14 publications

References 74 publications

Calreticulin expression and localization in plant cells during pollen–pistil interactions

Calreticulin expression and localization in plant cells during pollen–pistil interactions

Expression and localization of calreticulin in tobacco anthers and pollen tubes

The ER Folding Helpers: A Connection Between Protein Maturation, Stress Responses and Plant Development

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