The Maize Abscisic Acid-Responsive Protein Rab17 Is Located in the Nucleus and Interacts with Nuclear Localization Signals

Goday, Adela; Jensen, Anders B.; Culiáñez-Macià, Francisco A.; Alba, M. Mar; Figueras, Mercè; Serratosa, Joan; Torrent, Margarita; Pagès, Montserrat

doi:10.2307/3869755

Cited by 44 publications

(57 citation statements)

References 13 publications

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“…The nucleolar protein Noppl40 is also serine-rich and phosphorylated and is reported to shuttle between the nucleus and cytoplasm (31), although its role in import is unclear. Interestingly, Rabl7, a plant serine-rich phosphoprotein whose gene is expressed in response to the phytohormone abscisic acid also binds to NLSs via ligand blotting (32). Proteins identified as NBPs by other biochemical means include Hsc7O (33), which may have a role in nuclear import (34).…”

Section: Resultsmentioning

confidence: 99%

Nuclear localization signal binding proteins in higher plant nuclei.

Hicks

Raikhel

1995

Proc. Natl. Acad. Sci. U.S.A.

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Section: Resultsmentioning

confidence: 99%

Nuclear localization signal binding proteins in higher plant nuclei.

Hicks

Raikhel

1995

Proc. Natl. Acad. Sci. U.S.A.

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“…Several hypothetical roles have been proposed for Rab͞dehydrin proteins based on different experimental evidence, including binding to phosphate or sulfate ions (3), nuclear localization signal (NLS) peptides (4), calcium (5), and lipid vesicles containing acidic phospholipids (6), among others. All are aimed toward a protective role as chaperones to stabilize molecules or structures under stress conditions (4,7,8).Many proteins included in this Lea family contain the S domain (8), consisting of a tract of serines with several phosphorylation sites (9). Maize Rab17 protein is one of the most heavily phosphorylated proteins in mature embryos and is found both in nucleus and cytoplasm (4).…”

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confidence: 99%

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confidence: 99%

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Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize

Riera

Figueras

López

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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120

104

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The maize abscisic acid responsive protein Rab17 is a highly phosphorylated late embryogenesis abundant protein involved in plant responses to stress. In this study, we provide evidence of the importance of Rab17 phosphorylation by protein kinase CK2 in growth-related processes under stress conditions. We show the specific interaction of Rab17 with the CK2 regulatory subunits CK2␤-1 and CK2␤-3, and that these interactions do not depend on the phosphorylation state of Rab17. Live-cell fluorescence imaging of both CK2 and Rab17 indicates that the intracellular dynamics of Rab17 are regulated by CK2 phosphorylation. We found both CK2␤ subunits and Rab17 distributed over the cytoplasm and nucleus. By contrast, catalytic CK2␣ subunits and a Rab17 mutant protein (mRab17) that is not a substrate for CK2 phosphorylation remain accumulated in the nucleoli. A dual-color image shows that the CK2 holoenzyme accumulates mainly in the nucleus. The importance of Rab17 phosphorylation in vivo was assessed in transgenic plants. The overexpression of Rab17, but not mRab17, arrests the process of seed germination under osmotic stress conditions. Thus, the role of Rab17 in growth processes is mediated through its phosphorylation by protein kinase CK2. T he plant hormone abscisic acid (ABA) plays a major role in adaptation to osmotic stress and induces a number of genes that encode proteins generally assumed to be involved in protecting the cell and promoting recovery from stress. Proteins responsive to ABA accumulate during seed maturation; they naturally disappear during seed germination and can be induced to reappear by ABA treatment or osmotic stress in vegetative tissues (1, 2).Late embryogenesis abundant proteins (Lea) from group 2, responsive to ABA (Rab), or dehydrins are among the most common plant proteins involved in adaptation to water or osmotic stress. Several hypothetical roles have been proposed for Rab͞dehydrin proteins based on different experimental evidence, including binding to phosphate or sulfate ions (3), nuclear localization signal (NLS) peptides (4), calcium (5), and lipid vesicles containing acidic phospholipids (6), among others. All are aimed toward a protective role as chaperones to stabilize molecules or structures under stress conditions (4,7,8).Many proteins included in this Lea family contain the S domain (8), consisting of a tract of serines with several phosphorylation sites (9). Maize Rab17 protein is one of the most heavily phosphorylated proteins in mature embryos and is found both in nucleus and cytoplasm (4). The S domain of Rab17 is followed by a protein kinase CK2 phosphorylation consensus site (9). We previously established that Rab17 is phosphorylated by CK2 in serine residues of the S domain (10). Phosphorylation͞ dephosphorylation is an important mechanism that may regulate the function of Rab17 in the cell; however, the actual physiological function for Rab͞dehydrin proteins is still unknown, and a precise understanding of the function of Rab17 and the importance of its phosphorylation...

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“…This acidic serine region is immediately followed by another stretch of 30 amino acids containing 77% basic residues. Various nuclear localization signal (NLS) binding proteins contain similar domains (40,41).…”

Section: Molecular Cloning and Sequence Analysis Of The Matrin Cypmentioning

confidence: 99%

Matrin CYP, an SR-rich Cyclophilin That Associates with the Nuclear Matrix and Splicing Factors

Mortillaro

Berezney

1998

Journal of Biological Chemistry

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We report the identification and cloning of a nuclear matrix protein termed matrin cyclophilin or matrin CYP. The derived sequence of matrin cyp encodes a protein of 752 amino acids with a predicted mass of 88 kDa. A 172-residue stretch at the amino terminus shows high identity with the ubiquitous family of cyclophilins. Clustered throughout the carboxyl half of the protein are a series of serine-arginine (SR) repeats that are a characteristic feature of many RNA splicing factors. Antibodies raised against matrin CYP recognize a 106-kDa antigen that is detected in isolated nuclei and quantitatively subfractionates in the nuclear matrix. Laser scanning confocal microscopy localizes most of the anti-matrin CYP-specific antigen within the nucleus in a pattern of large bright speckles that co-localize with splicing factors and diffuse nucleoplasmic staining. A strikingly similar pattern of staining is observed in cells extracted for in situ nuclear matrices. A fusion protein containing the cyclophilin domain of matrin CYP exhibits cyclosporin A (CsA)-sensitive, peptidylprolyl cis-trans-isomerase activity that is characteristic of native cyclophilins. Although total rat liver nuclei contains predominantly CsA-resistant PPIase activity, the corresponding activity in the nuclear matrix is largely CsA-sensitive.The many functions associated with the cell nucleus are temporally and spatially regulated. Nuclear proteins and nucleic acids are often partitioned into functional domains (1). Examples include the nucleoli, heterochromatin, DNA replication sites (2, 3), and transcription domains (4, 5). In addition, a number of other domains have been identified that may also perform specific functions, such as the nuclear speckles (1, 6) and coiled (7) and promyelocytic leukemia (8 -10) bodies. Determining which molecules comprise these structures and how these molecules interact will lead to a greater understanding of the mechanisms responsible for their diverse functions and the role of nuclear architecture in these processes.The proteins and nucleic acids in the cell nucleus that resist solubilization by high salt extraction, nuclease digestion, and detergent solubilization constitute a structure termed the nuclear matrix (11,12). The isolated nuclear matrix has been shown to maintain a structure similar to and containing many of the functional properties associated with the nucleus (13).Several major proteins of the internal nuclear matrix have been identified by immunological methods and termed the nuclear matrins (14). The nuclear matrins include previously characterized proteins such as human RNP 1 A, human nRNP B (15), the nucleolar protein, B23/numatrin (14, 16), the hyperphosphorylated form of RNA pol II LS (17, 18), numerous SR-related proteins (19), and a 125-kDa acidic protein, termed matrin 3 (20). A recent study has confirmed the RNP nature of many of the major nuclear matrix proteins (21).Here we present results on the isolation of a cDNA that encodes an 88-kDa protein with a cyclophilin domain at the amino ter...

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The Maize Abscisic Acid-Responsive Protein Rab17 Is Located in the Nucleus and Interacts with Nuclear Localization Signals

Cited by 44 publications

References 13 publications

Nuclear localization signal binding proteins in higher plant nuclei.

Nuclear localization signal binding proteins in higher plant nuclei.

Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize

Matrin CYP, an SR-rich Cyclophilin That Associates with the Nuclear Matrix and Splicing Factors

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