Chaperoning the nuclear envelope

被引:0
作者
Kirstein, Janine [1 ]
机构
[1] Univ Bremen, Dept Cell Biol, Bremen, Germany
关键词
D O I
10.1038/s41556-022-01013-8
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
FG-nucleoporins of the nuclear pore complexes form a permeability barrier between the nucleus and the cytosol. FG-nucleoporins contain disordered regions and are prone to aggregation. Two studies identify the chaperone DNAJB6 as a key factor that prevents aggregation of FG-nucleoporins and assists in the biogenesis of nuclear pore complexes.
引用
收藏
页码:1563 / 1564
页数:2
相关论文
共 13 条
[1]   The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation [J].
Aprile, Francesco A. ;
Kallstig, Emma ;
Limorenko, Galina ;
Vendruscolo, Michele ;
Ron, David ;
Hansen, Christian .
SCIENTIFIC REPORTS, 2017, 7
[2]   The nuclear pore complex: understanding its function through structural insight [J].
Beck, Martin ;
Hurt, Ed .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2017, 18 (02) :73-89
[3]   Surface Properties Determining Passage Rates of Proteins through Nuclear Pores [J].
Frey, Steffen ;
Rees, Renate ;
Schuenemann, Juergen ;
Ng, Sheung Chun ;
Fuenfgeld, Kevser ;
Huyton, Trevor ;
Goerlich, Dirk .
CELL, 2018, 174 (01) :202-+
[4]   Dystonia-associated mutations cause premature degradation of torsinA protein and cell-type-specific mislocalization to the nuclear envelope [J].
Giles, Lisa M. ;
Chen, Jue ;
Li, Lian ;
Chin, Lih-Shen .
HUMAN MOLECULAR GENETICS, 2008, 17 (17) :2712-2722
[5]   The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model [J].
Kakkar, Vaishali ;
Mansson, Cecilia ;
de Mattos, Eduardo P. ;
Bergink, Steven ;
van der Zwaag, Marianne ;
van Waarde, Maria A. W. H. ;
Kloosterhuis, Niels J. ;
Melki, Ronald ;
van Cruchten, Remco T. P. ;
Al-Karadaghi, Salam ;
Arosio, Paolo ;
Dobson, Christopher M. ;
Knowles, Tuomas P. J. ;
Bates, Gillian P. ;
van Deursen, Jan M. ;
Linse, Sara ;
van de Sluis, Bart ;
Emanuelsson, Cecilia ;
Kampinga, Harm H. .
MOLECULAR CELL, 2016, 62 (02) :272-283
[6]   The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis [J].
Kuiper, E. F. Elsiena ;
Gallardo, Paola ;
Bergsma, Tessa ;
Mari, Muriel ;
Musskopf, Maiara Kolbe ;
Kuipers, Jeroen ;
Giepmans, Ben N. G. ;
Steen, Anton ;
Kampinga, Harm H. ;
Veenhoff, Liesbeth M. ;
Bergink, Steven .
NATURE CELL BIOLOGY, 2022, 24 (11) :1584-+
[7]   J-domain proteins interaction with neurodegenerative disease-related proteins [J].
Mariscal, Sara Maria Ayala ;
Kirstein, Janine .
EXPERIMENTAL CELL RESEARCH, 2021, 399 (02)
[8]   Amyloid-? oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation [J].
Osterlund, Nicklas ;
Lundqvist, Martin ;
Ilag, Leopold L. ;
Graslund, Astrid ;
Emanuelsson, Cecilia .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2020, 295 (24) :8135-8144
[9]   Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities [J].
Prophet, Sarah M. ;
Rampello, Anthony J. ;
Niescier, Robert F. ;
Gentile, Juliana E. ;
Mallik, Sunanda ;
Koleske, Anthony J. ;
Schlieker, Christian .
NATURE CELL BIOLOGY, 2022, 24 (11) :1630-+
[10]   Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2 [J].
Rampello, Anthony J. ;
Laudermilch, Ethan ;
Vishnoi, Nidhi ;
Prophet, Sarah M. ;
Shao, Lin ;
Zhao, Chenguang ;
Lusk, C. Patrick ;
Schlieker, Christian .
JOURNAL OF CELL BIOLOGY, 2020, 219 (06)