KEGG   PATHWAY: map04141
Entry
map04141                    Pathway                                

Name
Protein processing in endoplasmic reticulum
Description
The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
Class
Genetic Information Processing; Folding, sorting and degradation
Pathway map
map04141  Protein processing in endoplasmic reticulum
map04141

Disease
H00078  Frontotemporal lobar degeneration
H00118  Congenital disorders of glycosylation type I
H00221  Combined deficiency of factors V and VIII
H00344  Leprosy
H00409  Type 2 diabetes mellitus
H00545  Polycystic liver disease
H00594  Distal myopathy
H00595  Myofibrillar myopathies
H00740  Ichthyosis follicularis, alopecia, and photophobia syndrome
H00766  Wolcott-Rallison syndrome
H00854  Wolfram syndrome
H00917  Congenital dyserythropoietic anemias (CDAs)
H00927  Chylomicron retention disease
H01105  Cranio-lenticulo-sutural dysplasia
H01202  Cataract
H01284  Marinesco-Sjogren syndrome
H01478  Machado-Joseph disease
H01572  Cole-Carpenter syndrome
H02276  Kufs disease
H02287  Deafness, dystonia, and cerebral hypomyelination
H02430  Ataxia, combined cerebellar and peripheral, with hearing loss and diabetes mellitus
Other DBs
GO: 0030433 0034976
Reference
  Authors
Naidoo N
  Title
ER and aging-Protein folding and the ER stress response.
  Journal
Ageing Res Rev 8:150-9 (2009)
DOI:10.1016/j.arr.2009.03.001
Reference
  Authors
Malhotra JD, Kaufman RJ
  Title
The endoplasmic reticulum and the unfolded protein response.
  Journal
Semin Cell Dev Biol 18:716-31 (2007)
DOI:10.1016/j.semcdb.2007.09.003
Reference
  Authors
Maattanen P, Gehring K, Bergeron JJ, Thomas DY
  Title
Protein quality control in the ER: the recognition of misfolded proteins.
  Journal
Semin Cell Dev Biol 21:500-11 (2010)
DOI:10.1016/j.semcdb.2010.03.006
Reference
  Authors
Stolz A, Wolf DH
  Title
Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell.
  Journal
Biochim Biophys Acta 1803:694-705 (2010)
DOI:10.1016/j.bbamcr.2010.02.005
Reference
  Authors
Dejgaard K, Theberge JF, Heath-Engel H, Chevet E, Tremblay ML, Thomas DY
  Title
Organization of the Sec61 translocon, studied by high resolution native electrophoresis.
  Journal
J Proteome Res 9:1763-71 (2010)
DOI:10.1021/pr900900x
Related
pathway
map00510  N-Glycan biosynthesis
map03050  Proteasome
map03060  Protein export
map04210  Apoptosis
map04930  Type II diabetes mellitus
map05010  Alzheimer disease
map05012  Parkinson disease
map05020  Prion disease
KO pathway
ko04141   
LinkDB

DBGET integrated database retrieval system