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Nuclear localization sequence
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A nuclear localization signal or sequence (NLS) is an amino acid sequence that 'tags' a protein for import into the cell nucleus by nuclear transport. Typically, this signal consists of one or more short sequences of positively charged lysines or arginines exposed on the protein surface. Different nuclear localized proteins may share the same NLS. An NLS has the opposite function of a nuclear export signal (NES), which targets proteins out of the nucleus.
Contents
[hide]
1 Types
1.1 Classical
1.2 Non-classical
2 Discovery
3 Mechanism of nuclear import
4 See also
5 References
6 Further reading
7 External links
Types[edit]
Classical[edit]
These types of NLSs can be further classified as either monopartite or bipartite. The major structural differences between the two is that the two basic amino acid clusters in bipartite NLSs are separated by a relatively short spacer sequence (hence bipartite - 2 parts), while monopartite NLSs are not. The first NLS to be discovered was the sequence PKKKRKV in the SV40 Large T-antigen (a monopartite NLS).[1] The NLS of nucleoplasmin, KR[PAATKKAGQA]KKKK, is the prototype of the ubiquitous bipartite signal: two clusters of basic amino acids, separated by a spacer of about 10 amino acids.[2] Both signals are recognized by importin α. Importin α contains a bipartite NLS itself, which is specifically recognized by importin β. The latter can be considered the actual import mediator.
Chelsky et al. proposed the consensus sequence K-K/R-X-K/R for monopartite NLSs.[2] A Chelsky sequence may, therefore, be part of the downstream basic cluster of a bipartite NLS. Makkerh et al. carried out comparative mutagenesis on the nuclear localization signals of SV40 T-Antigen (monopartite), C-myc (monopartite), and nucleoplasmin (bipartite), and showed amino acid features common to all three. The role of neutral and acidic amino acids was shown for the first time in contributing to the efficiency of the NLS.[3]
Rotello et al. compared the nuclear localization efficiencies of eGFP fused NLSs of SV40 Large T-Antigen, Nucleoplasmin (AVKRPAATKKAGQAKKKKLD), EGL-13 (MSRRRKANPTKLSENAKKLAKEVEN), c-Myc (PAAKRVKLD) and TUS-protein (KLKIKRPVK) through rapid intracellular protein delivery. They found significantly higher nuclear localization efficiency of c-Myc NLS compared to that of SV40 NLS.[4]
Non-classical[edit]
There are many other types of NLS, such as the acidic M9 domain of hnRNP A1, the sequence KIPIK in yeast transcription repressor Matα2, and the complex signals of U snRNPs. Most of these NLSs appear to be recognized directly by specific receptors of the importin β family without the intervention of an importin α-like protein.[5]
A signal that appears to be specific for the massively produced and transported ribosomal proteins,[6][7] seems to come with a specialized set of importin β-like nuclear import receptors.[8]
Recently a class of NLSs known as PY-NLSs has been proposed, originally by Lee et al.[9] This PY-NLS motif, so named because of the proline-tyrosine amino acid pairing in it, allows the protein to bind to Importin β2 (also known as transportin or karyopherin β2), which then translocates the cargo protein into the nucleus. The structural basis for the binding of the PY-NLS contained in Importin β2 has been determined and an inhibitor of import designed.[10]
Discovery[edit]
The presence of the nuclear membrane that sequesters the cellular DNA is the defining feature of eukaryotic cells. The nuclear membrane, therefore, separates the nuclear processes of DNA replication and RNA transcription from the cytoplasmic process of protein production. Proteins required in the nucleus must be directed there by some mechanism. The first direct experimental examination of the ability of nuclear proteins to accumulate in the nucleus were carried out by John Gurdon when he showed that purified nuclear proteins accumulate in the nucleus of frog (Xenopus) oocytes after being micro-injected into the cytoplasm. These experiments were part of a series that subsequently led to studies of nuclear reprogramming, directly relevant to stem cell research.
The presence of several million pore complexes in the oocyte nuclear membrane and the fact that they appeared to admit many different molecules (insulin, bovine serum albumin, gold nanoparticles) led to the view that the pores are open channels and nuclear proteins freely enter the nucleus through the pore and must accumulate by binding to DNA or some other nuclear component. In other words, there was thought to be no specific transport mechanism.
This view was shown to be incorrect by Dingwall and Laskey in 1982. Using a protein called Nucleoplasmin, the archetypal ‘molecular chaperone’, they identified a domain in the protein that acts as a signal for nuclear entry.[11] This work stimulated research in the area, and two years later the first NLS was identified in SV40 Large T-antigen (or SV40, for short). However, a functional NLS could not be identified in another nuclear protein simply on the basis of similarity to the SV40 NLS. In fact, only a small percentage of cellular (non-viral) nuclear proteins contained a sequence similar to the SV40 NLS. A detailed examination of Nucleoplasmin identified a sequence with two elements made up of basic amino acids separated by a spacer arm. One of these elements was similar to the SV40 NLS but was not able to direct a protein to the cell nucleus when attached to a non-nuclear reporter protein. Both elements are required.[12] This kind of NLS has become known as a bipartite classical NLS. The bipartite NLS is now known to represent the major class of NLS found in cellular nuclear proteins[citation needed] and structural analysis has revealed how the signal is recognized by a receptor (importin α) protein[13] (the structural basis of some monopartite NLSs is also known[14]). Many of the molecular details of nuclear protein import are now known. This was made possible by the demonstration that nuclear protein import is a two-step process; the nuclear protein binds to the nuclear pore complex in a process that does not require energy. This is followed by an energy-dependent translocation of the nuclear protein through the channel of the pore complex.[15][16] By establishing the presence of two distinct steps in the process the possibility of identifying the factors involved was established and led on to the identification of the importin family of NLS receptors and the GTPase Ran.
Mechanism of nuclear import[edit]
Proteins gain entry into the nucleus through the nuclear envelope. The nuclear envelope consists of concentric membranes, the outer and the inner membrane. The inner and outer membranes connect at multiple sites, forming channels between the cytoplasm and the nucleoplasm. These channels are occupied by nuclear pore complexes (NPCs), complex multiprotein structures that mediate the transport across the nuclear membrane.
A protein translated with a NLS will bind strongly to importin (aka karyopherin), and, together, the complex will move through the nuclear pore. At this point, Ran-GTP will bind to the importin-protein complex, and its binding will cause the importin to lose affinity for the protein. The protein is released, and now the Ran-GTP/importin complex will move back out of the nucleus through the nuclear pore. A GTPase-activating protein (GAP) in the cytoplasm hydrolyzes the Ran-GTP to GDP, and this causes a conformational change in Ran, ultimately reducing its affinity for importin. Importin is released and Ran-GDP is recycled back to the nucleus where a Guanine nucleotide exchange factor (GEF) exchanges its GDP back for GTP.
See also[edit]
A nuclear export signal (NES) can direct a protein to be exported from the nucleus.
References[edit]
Jump up ^ Kalderon D, Roberts BL, Richardson WD, Smith AE (1984). "A short amino acid sequence able to specify nuclear location". Cell. 39 (3 Pt 2): 499–509. PMID 6096007. doi:10.1016/0092-8674(84)90457-4.
^ Jump up to: a b Dingwall C, Robbins J, Dilworth SM, Roberts B, Richardson WD (Sep 1988). "The nucleoplasmin nuclear location sequence is larger and more complex than that of SV-40 large T antigen". J Cell Biol. 107 (3): 841–9. PMC 2115281  . PMID 3417784. doi:10.1083/jcb.107.3.841.
Jump up ^ Makkerh JP, Dingwall C, Laskey RA (August 1996). "Comparative mutagenesis of nuclear localisation signals reveals the importance of neutral and acidic amino acids". Curr Biol. 6 (8): 1025–7. PMID 8805337. doi:10.1016/S0960-9822(02)00648-6.
Jump up ^ Ray M, Tang R, Jiang Z, Rotello VM (2015). "Quantitative tracking of protein trafficking to the nucleus using cytosolic protein delivery by nanoparticle-stabilized nanocapsules". Bioconjug. Chem. 26 (6): 1004–7. PMC 4743495  . PMID 26011555. doi:10.1021/acs.bioconjchem.5b00141.
Jump up ^ Mattaj IW, Englmeier L (1998). "Nucleocytoplasmic transport: the soluble phase". Annu Rev Biochem. 67 (1): 265–306. PMID 9759490. doi:10.1146/annurev.biochem.67.1.265.
Jump up ^ Timmers AC, Stuger R, Schaap PJ, van 't Riet J, Raué HA (June 1999). "Nuclear and nucleolar localisation of Saccharomyces cerevisiae ribosomal proteins S22 and S25". FEBS Lett. 452 (3): 335–40. PMID 10386617. doi:10.1016/S0014-5793(99)00669-9.
Jump up ^ Garrett RA, Douthwate SR, Matheson AT, Moore PB, Noller HF (2000). The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions. ASM Press. ISBN 978-1-55581-184-6.
Jump up ^ Rout MP, Blobel G, Aitchison JD (May 1997). "A distinct nuclear import pathway used by ribosomal proteins". Cell. 89 (5): 715–25. PMID 9182759. doi:10.1016/S0092-8674(00)80254-8.
Jump up ^ Lee BJ, Cansizoglu AE, Süel KE, Louis TH, Zhang Z, Chook YM (August 2006). "Rules for nuclear localisation sequence recognition by karyopherin beta 2". Cell. 126 (3): 543–58. PMC 3442361  . PMID 16901787. doi:10.1016/j.cell.2006.05.049.
Jump up ^ Cansizoglu AE, Lee BJ, Zhang ZC, Fontoura BM, Chook YM (May 2007). "Structure-based design of a pathway-specific nuclear import inhibitor". Nature Structural & Molecular Biology. 14 (5): 452–4. PMC 3437620  . PMID 17435768. doi:10.1038/nsmb1229.
Jump up ^ Dingwall C, Sharnick SV, Laskey RA (September 1982). "A polypeptide domain that specifies migration of nucleoplasmin into the nucleus". Cell. 30 (2): 449–58. PMID 6814762. doi:10.1016/0092-8674(82)90242-2.
Jump up ^ Dingwall C, Laskey RA (December 1991). "Nuclear targeting sequences--a consensus?". Trends in Biochemical Sciences. 16 (12): 478–81. PMID 1664152. doi:10.1016/0968-0004(91)90184-W.
Jump up ^ Conti E, Kuriyan J (March 2000). "Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localisation signals by karyopherin alpha". Structure. 8 (3): 329–38. PMID 10745017. doi:10.1016/s0969-2126(00)00107-6.
Jump up ^ Conti E, Uy M, Leighton L, Blobel G, Kuriyan J (July 1998). "Crystallographic analysis of the recognition of a nuclear localisation signal by the nuclear import factor karyopherin alpha". Cell. 94 (2): 193–204. PMID 9695948. doi:10.1016/S0092-8674(00)81419-1.
Jump up ^ Dingwall C, Robbins J, Dilworth SM, Roberts B, Richardson WD (September 1988). "The nucleoplasmin nuclear location sequence is larger and more complex than that of SV-40 large T antigen". The Journal of Cell Biology. 107 (3): 841–9. PMC 2115281  . PMID 3417784. doi:10.1083/jcb.107.3.841.
Jump up ^ Newmeyer DD, Forbes DJ (March 1988). "Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation". Cell. 52 (5): 641–53. PMID 3345567. doi:10.1016/0092-8674(88)90402-3.
Further reading[edit]
Görlich D (Jun 1997). "Nuclear protein import". Current Opinion in Cell Biology. 9 (3): 412–9. PMID 9159081. doi:10.1016/S0955-0674(97)80015-4.
Lusk CP, Blobel G, King MC (May 2007). "Highway to the inner nuclear membrane: rules for the road". Nature Reviews Molecular Cell Biology. 8 (5): 414–20. PMID 17440484. doi:10.1038/nrm2165.
External links[edit]
Eukaryotic Linear Motif resource motif class TRG_NLS_Bipartite_1
Eukaryotic Linear Motif resource motif class TRG_NLS_MonoCore_2
Eukaryotic Linear Motif resource motif class TRG_NLS_MonoExtC_3
Eukaryotic Linear Motif resource motif class TRG_NLS_MonoExtC_4
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Talia Shire
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Talia Shire
Shire in Rich Man, Poor Man (1976)
Born
Talia Rose Coppola
(1946-04-25) April 25, 1946 (age 72)
Lake Success, New York, U.S.
Occupation
Actress
Years active
1968–present
Spouse(s)
David Shire
(m. 1970; div. 1980)
Jack Schwartzman
(m. 1980; d. 1994)
Children
3, including Jason and Robert
Parent(s)
Carmine Coppola
Italia Pennino
Relatives
August Coppola (brother)
Francis Ford Coppola (brother)
Jason Schwartzman (son)
Robert Schwartzman (son)
John Schwartzman (stepson)
Nicolas Cage (nephew)
Sofia Coppola (niece)
Family
Coppola
Talia Rose Shire (née Coppola; born April 25, 1946) is an American actress best known for her roles as Connie Corleone in The Godfather films and Adrian Balboa in the Rocky series. For her work in The Godfather Part II and Rocky, Shire was nominated for two Academy Awards for Best Supporting Actress and Best Actress, respectively, and for the Golden Globe Award for Best Actress in a Drama for her role in Rocky.
Contents
[hide]
1 Personal life
2 Career
3 Filmography
4 See also
5 References
6 External links
Personal life[edit]
Shire was born Talia Rose Coppola in Lake Success, New York, the only daughter of Italia (née Pennino; 1912–2004) and arranger/composer Carmine Coppola (1910–1991). Her parents were both of Italian descent. Talia is the sister of director and producer Francis Ford Coppola and academic August Coppola, the aunt of actor Nicolas Cage and director Sofia Coppola, and the niece of composer and conductor Anton Coppola.[1] She has three children. Her son Matthew Orlando Shire is the child of her first marriage to composer David Shire. Her other sons, actors/musicians Jason and Robert, are from her second marriage, to the late film producer Jack Schwartzman.[2]
Career[edit]
Shire portrayed Connie Corleone in The Godfather and its sequels. She was nominated for the Academy Award for Best Supporting Actress for her performance in 1974's The Godfather: Part II. In 1976, she portrayed Adrian Pennino, the love interest of Rocky Balboa in Rocky. For this role, she won the New York Film Critics Circle Award for Best Supporting Actress, the National Board of Review Award for Best Supporting Actress, and was nominated for both the Golden Globe Award for Best Actress in a Drama and the Academy Award for Best Actress. In addition to four Rocky sequels, Shire has appeared in such films as Kiss the Bride (2002), I Heart Huckabees (2004), and Homo Erectus (2007).[3]
Filmography[edit]
Films
Year
Title
Role
Notes
1968 The Wild Racers 1st Girlfriend
1970 The Dunwich Horror Nurse Cora
Maxie Sandy
1971 Gas-s-s-s Coralee
The Christian Licorice Store Last Party Guest
1972 The Godfather Connie Corleone
The Outside Man Make-Up Girl
1974 The Godfather Part II Connie Corleone Nominated – Academy Award for Best Supporting Actress
1976 Rocky Adrian Pennino National Board of Review Award for Best Supporting Actress
New York Film Critics Circle Award for Best Supporting Actress
National Society of Film Critics Award for Best Supporting Actress (2nd place)
Nominated – Academy Award for Best Actress
Nominated – Golden Globe Award for Best Actress - Motion Picture Drama
1979 Old Boyfriends Dianne Cruise
Prophecy Maggie Verne
Rocky II Adrian Pennino/Balboa
1980 Windows Emily Hollander
1982 Rocky III Adrian Pennino/Balboa
1985 Rocky IV Adrian Pennino/Balboa
1986 Rad Mrs. Jones
Hyper Sapien: People from Another Star Dr. Tedra Rosen
1989 New York Stories Charlotte Segment: Life Without Zoe
1990 Rocky V Adrian Pennino/Balboa
The Godfather Part III Connie Corleone
1991 Cold Heaven Sister Martha
1992 Bed & Breakfast Claire
1993 Deadfall Sam
1997 A River Made to Drown In Jaime's Mother
She's So Lovely Restaurant Owner Uncredited Role
1998 Divorce: A Contemporary Western Lacey
Can I Play? Robert Short film
Caminho dos Sonhos Ida Stern
The Landlady Melanie Leroy
1999 Lured Innocence Martha Chambers
Palmer's Pick Up Mr. Price
1999 The Black And The White Tulip Clayton
2000 The Visit Parole Board Member Marilyn
2001 The Whole Shebang Countess Bazinni
2002 Kiss the Bride Irena Sposato
2003 Family Tree Patricia Short film
Dunsmore Mildred Green
2004 I ♥ Huckabees Mrs. Silver
2005 Pomegranate Aunt Sophia
2007 Homo Erectus Ishbo's Mother
2008 Looking for Palladin Rosario
Dim Sum Funeral Viola Gruber
My Father's Will
2009 The Deported Dina
2010
Minkow Carole Minkow
Scratching the Surface Mrs. Shifman
2011 The Return of Joe Rich Gloria Neiderman
2013 Palo Alto Mrs. Ganem
2016 Dreamland Victoria
Television
Year
Title
Role
Notes
1975 Foster and Laurie Adelaide Laurie CBS TV-Movie
1976 Doctors' Hospital Episode: Lullabye
Rich Man, Poor Man Teresa Santoro ABC Miniseries
1977 Kill Me If You Can Rosalie Asher NBC TV-Movie
The Godfather Saga Connie Corleone NBC TV-Movie
1978 Daddy, I Don't Like It Like This Carol Agnelli CBS TV-Movie
1987 Blood Vows: The Story of a Mafia Wife Gina NBC TV-Movie
Faerie Tale Theatre Wilma Van Winkle Episode: Rip Van Winkle
1991 Mark Twain and Me Jean Clemens TV-Movie
1992 For Richer, for Poorer Millie Katourian HBO TV-Movie
CBS Schoolbreak Special Mrs. Leland Episode: Please, God, I'm Only Seventeen
1993 Chantilly Lace Maggie Showtime TV-Movie
1995 Blossom Herself Episode: A Star Is Bared
1997 Born Into Exile Donna Nolan NBC TV-Movie
2007 Blue Smoke Bianca Hale Lifetime TV-Movie
Christmas at Cadillac Jack's Peg TV-Movie
2017 Kingdom Annette Kulina Episodes: "Old Pueblo" and "Cactus"
2018 Grace and Frankie Teddie Episodes: "The Pop-Ups" and "The Hinge"
See also[edit]
Coppola family tree
Francis Ford Coppola
References[edit]
Jump up ^ "If Hollywood Royalty Exists, It Begins With The Coppola Family". Film School Rejects. June 25, 2017. Retrieved March 17, 2018.
Jump up ^ Talia Shire profile, filmreference.com; accessed November 8, 2015.
Jump up ^ Profile; retrieved April 30, 2009
External links[edit]
Talia Shire on IMDb
[show]
Awards for Talia Shire
[show]
v
t
e
National Board of Review Award for Best Supporting Actress
Nina Foch (1954)
Marjorie Rambeau (1955)
Debbie Reynolds (1956)
Sybil Thorndike (1957)
Kay Walsh (1958)
Edith Evans (1959)
Shirley Jones (1960)
Ruby Dee (1961)
Angela Lansbury (1962)
Margaret Rutherford (1963)
Edith Evans (1964)
Joan Blondell (1965)
Vivien Merchant (1966)
Marjorie Rhodes (1967)
Virginia Maskell (1968)
Pamela Franklin (1969)
Karen Black (1970)
Cloris Leachman (1971)
Marisa Berenson (1972)
Sylvia Sidney (1973)
Valerie Perrine (1974)
Ronee Blakley (1975)
Talia Shire (1976)
Diane Keaton (1977)
Angela Lansbury (1978)
Meryl Streep (1979)
Eva Le Gallienne (1980)
Mona Washbourne (1981)
Glenn Close (1982)
Linda Hunt (1983)
Sabine Azéma (1984)
Anjelica Huston (1985)
Dianne Wiest (1986)
Olympia Dukakis (1987)
Frances McDormand (1988)
Mary Stuart Masterson (1989)
Winona Ryder (1990)
Kate Nelligan (1991)
Judy Davis (1992)
Winona Ryder (1993)
Rosemary Harris (1994)
Mira Sorvino (1995)
Juliette Binoche / Kristin Scott Thomas (1996)
Anne Heche (1997)
Christina Ricci (1998)
Julianne Moore (1999)
Lupe Ontiveros (2000)
Cate Blanchett (2001)
Kathy Bates (2002)
Patricia Clarkson (2003)
Laura Linney (2004)
Gong Li (2005)
Catherine O'Hara (2006)
Amy Ryan (2007)
Penélope Cruz (2008)
Anna Kendrick (2009)
Jacki Weaver (2010)
Shailene Woodley (2011)
Ann Dowd (2012)
Octavia Spencer (2013)
Jessica Chastain (2014)
Jennifer Jason Leigh (2015)
Naomie Harris (2016)
Laurie Metcalf (2017)
[show]
v
t
e
New York Film Critics Circle Award for Best Supporting Actress
Dyan Cannon (1969)
Karen Black (1970)
Ellen Burstyn (1971)
Jeannie Berlin (1972)
Valentina Cortese (1973)
Valerie Perrine (1974)
Lily Tomlin (1975)
Talia Shire (1976)
Sissy Spacek (1977)
Maureen Stapleton (1978)
Meryl Streep (1979)
Mary Steenburgen (1980)
Mona Washbourne (1981)
Jessica Lange (1982)
Linda Hunt (1983)
Christine Lahti (1984)
Anjelica Huston (1985)
Dianne Wiest (1986)
Vanessa Redgrave (1987)
Diane Venora (1988)
Lena Olin (1989)
Jennifer Jason Leigh (1990)
Judy Davis (1991)
Miranda Richardson (1992)
Gong Li (1993)
Dianne Wiest (1994)
Mira Sorvino (1995)
Courtney Love (1996)
Joan Cusack (1997)
Lisa Kudrow (1998)
Catherine Keener (1999)
Marcia Gay Harden (2000)
Helen Mirren (2001)
Patricia Clarkson (2002)
Shohreh Aghdashloo (2003)
Virginia Madsen (2004)
Maria Bello (2005)
Jennifer Hudson (2006)
Amy Ryan (2007)
Penélope Cruz (2008)
Mo'Nique (2009)
Melissa Leo (2010)
Jessica Chastain (2011)
Sally Field (2012)
Jennifer Lawrence (2013)
Patricia Arquette (2014)
Kristen Stewart (2015)
Michelle Williams (2016)
Tiffany Haddish (2017)
[show]
v
t
e
Coppola family
1st generation
Carmine Coppola
Anton Coppola
Italia Coppola
2nd generation
August Coppola
Francis Ford Coppola
Talia Shire
Eleanor Coppola
Jack Schwartzman
3rd generation
Nicolas Cage
Jason Schwartzman
Robert Coppola Schwartzman
Sofia Coppola
Roman Coppola
Gian-Carlo Coppola
Marc Coppola
Christopher Coppola
4th generation
Gia Coppola
See also
Palazzo Margherita (Bernalda)
Authority control
WorldCat Identities
VIAF: 49420573
LCCN: n94005244
ISNI: 0000 0001 1443 5855
GND: 129186929
SUDOC: 059671602
BNF: cb14014568w (data)
BIBSYS: 99014302
BNE: XX1262012
SNAC: w6mq80pn
Retrieved from "https://en.wikipedia.org/w/index.php?title=Talia_Shire&oldid=836266320"
Categories:
1946 births
Living people
People from North Hempstead, New York
American people of Italian descent
American people of Lucanian descent
American Roman Catholics
American film actresses
Coppola family
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20th-century American actresses
21st-century American actresses
Actresses of Italian descent
People of Campanian descent
People from Lake Success, New York
Hidden categories:
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