KEGG   PATHWAY: gla04141
Entry
gla04141                    Pathway                                
Name
Protein processing in endoplasmic reticulum - Giardia lamblia
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
gla04141  Protein processing in endoplasmic reticulum
gla04141

Other DBs
GO: 0030433 0034976
Organism
Giardia lamblia [GN:gla]
Gene
GL50803_003896  Sec61-gamma [KO:K07342]
GL50803_00137685  Dolichyl-diphosphooligosaccharide--protein glycosyltransferase [KO:K07151] [EC:2.4.99.18]
GL50803_0014843  Chaperone protein dnaJ [KO:K09523]
GL50803_0015247  Glucose regulated protein 94 / Heat shock protein 90 [KO:K09487]
GL50803_007569  GTP-binding protein Sar1 [KO:K07953] [EC:3.6.5.-]
GL50803_002562  Sec31 [KO:K14005]
GL50803_009376  Sec23 [KO:K14006]
GL50803_0017164  Sec24-like 1 [KO:K14007]
GL50803_0017065  Sec24-like 3 [KO:K14007]
GL50803_009413  Protein disulfide isomerase PDI2 [KO:K09580] [EC:5.3.4.1]
GL50803_0029487  Protein disulfide isomerase [KO:K09584] [EC:5.3.4.1]
GL50803_0015126  Derlin-like protein [KO:K13989]
GL50803_0012885  UBA-like domain-containing protein [KO:K14012]
GL50803_0016867  AAA family ATPase [KO:K13525]
GL50803_0094658  NPL4-like protein [KO:K14015]
GL50803_003994  Ubiquitin fusion degradation protein 1 [KO:K14016]
GL50803_0088765  Cytosolic heat shock protein 70 [KO:K03283]
GL50803_0017483  Chaperone protein DnaJ subfamily B [KO:K09507]
GL50803_0015089  hypothetical protein [KO:K09562]
GL50803_0015270  putative Ubiquitin protein [KO:K04523]
GL50803_0012089  Kinase, PEK [KO:K08860] [EC:2.7.11.1]
GL50803_0013943  Eukaryotic translation initiation factor 2 alpha subunit [KO:K03237]
GL50803_003171  Ubiquitin-conjugating enzyme E2 G1 [KO:K10575] [EC:2.3.2.23]
Compound
C00076  Calcium cation
G00009   
G00010   
G00011   
G00012   
G10694   
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
gla00510  N-Glycan biosynthesis
gla03050  Proteasome
gla03060  Protein export
KO pathway
ko04141   

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