1. Latency-associated protein*
2. TGFB1

Identifiers
NAME:Latency-associated protein*:TGFB1

Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
 EMT Senescence   / EMT_REGULATORS 
 EMT Senescence   / ECM 

References
PMID:20519943
PMID:17934056
PMID:16474430
PMID:14557817
PMID:21900405
TGFB inhibits proliferation
TGFB overproduction causes fibrosis.
Each TGFB gene encodes a preproprotein sequence consisting of a signal peptide, a propeptide (LAP) and the mature TGFB
After translocation into the endoplamic reticulum, TGFB proprotein monomers form homomdimers liked by disulfide bonds, forming pro-TGFB
In the Golgi, the prodomains undergo glycosylation.
Also in the Golgi, FURIN hydolyzes the leavage site from LAP, creating TGFB and LAP-derived homodimers
The 2 homodimers remain noncovalently associated and are secreted.
The LAP-derived homodimer prevents TGFB from binding TGFB receptors.

Identifiers
NAME:Latency-associated protein*:TGFB1

Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
 EMT Senescence   / EMT_REGULATORS 
 EMT Senescence   / ECM 

References
PMID:20519943
PMID:17934056
PMID:16474430
PMID:14557817
PMID:21900405
TGFB inhibits proliferation
TGFB overproduction causes fibrosis.
Each TGFB gene encodes a preproprotein sequence consisting of a signal peptide, a propeptide (LAP) and the mature TGFB
After translocation into the endoplamic reticulum, TGFB proprotein monomers form homomdimers liked by disulfide bonds, forming pro-TGFB
In the Golgi, the prodomains undergo glycosylation.
Also in the Golgi, FURIN hydolyzes the leavage site from LAP, creating TGFB and LAP-derived homodimers
The 2 homodimers remain noncovalently associated and are secreted.
The LAP-derived homodimer prevents TGFB from binding TGFB receptors.

Identifiers
NAME:Latency-associated protein*:TGFB1

Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
 EMT Senescence   / EMT_REGULATORS 
 EMT Senescence   / ECM 

References
PMID:20519943
PMID:17934056
PMID:16474430
PMID:14557817
PMID:21900405
TGFB inhibits proliferation
TGFB overproduction causes fibrosis.
Each TGFB gene encodes a preproprotein sequence consisting of a signal peptide, a propeptide (LAP) and the mature TGFB
After translocation into the endoplamic reticulum, TGFB proprotein monomers form homomdimers liked by disulfide bonds, forming pro-TGFB
In the Golgi, the prodomains undergo glycosylation.
Also in the Golgi, FURIN hydolyzes the leavage site from LAP, creating TGFB and LAP-derived homodimers
The 2 homodimers remain noncovalently associated and are secreted.
The LAP-derived homodimer prevents TGFB from binding TGFB receptors.

1. Latency-associated protein*:​TGFB1@Extracellular space
2. Latency-associated protein*|​hm2:​TGFB1|​hm2@Extracellular space
3. Latency-associated protein*|​hm2:​TGFB1|​hm2@Extracellular space

1. Latency-associated protein*|​hm2@Extracellular space + TGFB1|​hm2|​active@Extracellular space → Latency-associated protein*|​hm2:​TGFB1|​hm2@Extracellular space
2. Latency-associated protein*|​hm2:​TGFB1|​hm2@Extracellular space + LTBP1@Extracellular space → LTBP1:​Latency-associated protein*|​hm2:​TGFB1|​hm2@Extracellular space
3. Latency-associated protein*|​hm2:​TGFB1|​hm2@Extracellular space → Latency-associated protein*|​hm2@Extracellular space + TGFB1|​hm2|​active@Extracellular space
4. Latency-associated protein*:​TGFB1@Extracellular space → Latency-associated protein*|​hm2:​TGFB1|​hm2@Extracellular space