Mechanisms of the Hsp70 chaperone system.
Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release. The Hsp40 co-chaperones stimulate ATP hydrolysis by Hsp70 and the type 1 Hsp40 proteins are conserved from Escherichia coli to humans. Various nucleotide exchange factors also promote the Hsp70 ATPase cycle. Recent advances have added to our understanding of the Hsp70 mechanism at a molecular level.
Young
Jason C
JC
Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, QC H3G 1Y6, Canada.
D000255:Adenosine Triphosphate / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000378:metabolism
D018840:HSP70 Heat-Shock Proteins; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase
J Mol Biol. 1996 Jul 12;260(2):224-35
8764402
J Biol Chem. 2006 Sep 8;281(36):26235-44
16854979
J Biol Chem. 2005 Apr 8;280(14):13671-81
15661747
J Biol Chem. 2005 Jan 7;280(1):695-702
15496404
Structure. 2003 Dec;11(12):1475-83
14656432
J Mol Biol. 1999 Feb 26;286(3):915-32
10024459
J Cell Biol. 1997 Dec 1;139(5):1089-95
9382858
Cell. 1998 Feb 6;92(3):351-66
9476895
J Biol Chem. 2008 Apr 4;283(14):8877-84
18218635
Cell. 2008 Jun 13;133(6):1068-79
18555782
Nat Struct Biol. 2000 Jul;7(7):586-93
10876246
Mol Cell. 2005 Nov 23;20(4):513-24
16307916
J Biol Chem. 2006 Mar 17;281(11):7479-88
16415343
Science. 1996 Jun 14;272(5268):1606-14
8658133
Biochemistry. 2006 Dec 19;45(50):15075-84
17154545
Cell Stress Chaperones. 1998 Mar;3(1):28-36
9585179
EMBO J. 2006 Jun 7;25(11):2519-28
16688212
J Biol Chem. 2003 Nov 7;278(45):44457-66
12941935
Nat Struct Mol Biol. 2008 Dec;15(12):1309-17
19029896
Mol Biol Cell. 2004 Feb;15(2):761-73
14657253
Proc Natl Acad Sci U S A. 2009 May 26;106(21):8471-6
19439666
J Mol Biol. 2005 Mar 4;346(4):1005-11
15701512
J Biol Chem. 2000 Aug 11;275(32):24728-34
10816573
Cell Mol Life Sci. 2006 Nov;63(22):2560-70
16952052
J Biol Chem. 1996 Jun 21;271(25):14840-8
8662861
Protein Sci. 2006 Feb;15(2):223-33
16384998
J Biol Chem. 2001 Aug 31;276(35):32538-44
11441021
Biochem J. 2005 Mar 15;386(Pt 3):453-60
15500443
Science. 2002 Mar 8;295(5561):1852-8
11884745
J Biol Chem. 2006 Dec 15;281(50):38705-11
17052976
Mol Cell. 2006 Feb 3;21(3):359-67
16455491
Cell Mol Life Sci. 2005 Mar;62(6):670-84
15770419
Mol Cell. 2008 Jul 25;31(2):232-43
18550409
J Biol Chem. 2003 May 23;278(21):19038-43
12654915
Mol Biol Cell. 2002 Aug;13(8):2760-70
12181344
J Biochem. 2004 Feb;135(2):193-200
15047721
J Mol Biol. 2008 Oct 31;383(1):155-66
18723025
FEBS Lett. 2002 Nov 6;531(2):339-42
12417338
EMBO J. 2008 Nov 5;27(21):2862-72
18923430
Cell. 2007 Oct 5;131(1):106-20
17923091
Science. 2001 Feb 23;291(5508):1553-7
11222862
Protein Sci. 2005 Jul;14(7):1697-709
15987899
J Biol Chem. 2006 Jun 16;281(24):16493-501
16613854
Nature. 1990 Aug 16;346(6285):623-8
2143562
Trends Biochem Sci. 2003 Oct;28(10):541-7
14559183
FEBS Lett. 2007 Jul 31;581(19):3702-10
17544402
FEBS Lett. 2001 May 18;497(1):55-8
11376662
Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10345-9
7937953
EMBO J. 2005 Feb 9;24(3):611-22
15660130
Mol Cell Biol. 2000 May;20(9):3027-36
10757787
J Biol Chem. 2006 Jan 20;281(3):1605-11
16275641
Mol Cell. 2007 Apr 13;26(1):27-39
17434124
J Biol Chem. 2008 Oct 3;283(40):27100-9
18684711
Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11073-8
19549854
J Biol Chem. 1999 Nov 26;274(48):34045-52
10567371
Mol Biol Cell. 2008 Dec;19(12):5249-58
18829866
J Mol Biol. 2005 May 27;349(1):163-83
15876376
EMBO J. 2006 Jun 7;25(11):2510-8
16688211
Mol Cell. 2005 Feb 4;17(3):367-79
15694338
Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7163-8
17438278
J Biol Chem. 2009 Feb 6;284(6):3628-39
19056735
Nat Rev Mol Cell Biol. 2004 Oct;5(10):781-91
15459659
Proc Natl Acad Sci U S A. 1999 May 11;96(10):5452-7
10318904
EMBO Rep. 2004 Jun;5(6):567-71
15170475
Nat Struct Biol. 2000 Apr;7(4):298-303
10742174
EMBO J. 2008 Nov 5;27(21):2873-82
18923428
Nat Struct Biol. 2001 May;8(5):427-32
11323718
EMBO J. 1993 Nov;12(11):4137-44
7900997
J Biol Chem. 1998 Mar 6;273(10):5970-8
9488737
Mol Biol Cell. 2007 Sep;18(9):3414-28
17596514
Proc Natl Acad Sci U S A. 2008 Oct 28;105(43):16519-24
18948593
J Biol Chem. 2008 May 30;283(22):15502-11
18400763
Cell. 2003 Jan 10;112(1):41-50
12526792
Mol Cell. 2007 Nov 9;28(3):422-33
17996706
Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2874-8
1826368
Nat Cell Biol. 2001 Oct;3(10):E237-41
11584289
J Cell Biol. 2001 Feb 19;152(4):851-6
11266475
J Biol Chem. 1997 Dec 12;272(50):31636-40
9395504
Science. 1997 Apr 18;276(5311):431-5
9103205
EMBO J. 1997 Oct 15;16(20):6209-16
9321400
EMBO J. 1999 Mar 15;18(6):1492-505
10075921