Tjp1

This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family of proteins, and acts as a tight junction adaptor protein that also regulates adherens junctions. Tight junctions regulate the movement of ions and macromolecules between endothelial and epithelial cells. The multidomain structure of this scaffold protein, including a postsynaptic density 95/disc-large/zona occludens (PDZ) domain, a Src homology (SH3) domain, a guanylate kinase (GuK) domain and unique (U) motifs all help to co-ordinate binding of transmembrane proteins, cytosolic proteins, and F-actin, which are required for tight junction function. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Aug 2017]

tight junction protein 1

TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688).
The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity).
Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187).
Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113).
With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity).

Biological Process actomyosin structure organizationSource:ARUK-UCL1 Publication
Biological Process adherens junction maintenanceSource:ARUK-UCL1 Publication
Biological Process cell-cell adhesionSource:GO_Central1 Publication
Biological Process cell-cell junction assemblySource:ProtInc1 Publication
Biological Process cell-cell junction organizationSource:ARUK-UCL1 Publication
Biological Process establishment of endothelial intestinal barrierSource:UniProtKB1 Publication
Biological Process maintenance of blood-brain barrierSource:ARUK-UCL1 Publication
Biological Process negative regulation of actin cytoskeleton reorganizationSource:ARUK-UCL1 Publication
Biological Process negative regulation of apoptotic processSource:ARUK-UCL1 Publication
Biological Process negative regulation of stress fiber assemblySource:ARUK-UCL
Biological Process positive regulation of blood-brain barrier permeabilitySource:ARUK-UCL1 Publication
Biological Process positive regulation of cell migrationSource:ARUK-UCL1 Publication
Biological Process positive regulation of cell population proliferationSource:ARUK-UCL1 Publication
Biological Process positive regulation of cell-cell adhesion mediated by cadherinSource:ARUK-UCL1 Publication
Biological Process positive regulation of sprouting angiogenesisSource:ARUK-UCL1 Publication
Biological Process protein localization to adherens junctionSource:ARUK-UCL1 Publication
Biological Process protein localization to bicellular tight junctionSource:ARUK-UCL1 Publication
Biological Process protein localization to cell-cell junctionSource:ARUK-UCL1 Publication
Biological Process regulation of bicellular tight junction assemblySource:ARUK-UCL1 Publication
Biological Process regulation of cell junction assemblySource:ARUK-UCL1 Publication
Biological Process regulation of cytoskeleton organizationSource:ARUK-UCL1 Publication

Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (PubMed:19332538, PubMed:7542259).
This response is dependent on an intact actin microfilament system (PubMed:7542259).
Dephosphorylated by PTPRJ (PubMed:19332538).