Search results for RAB5A

Showing 15 results out of 15

×

Species

Types

Compartments

Reaction types

Search properties

Species

Types

Compartments

Reaction types

Search properties

Protein (6 results from a total of 6)

Identifier: R-HSA-2201187
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RAB5A: P20339
Identifier: R-HSA-452257
Species: Homo sapiens
Compartment: endosome membrane
Primary external reference: UniProt: RAB5A: P20339
Identifier: R-HSA-2130175
Species: Homo sapiens
Compartment: early endosome membrane
Primary external reference: UniProt: RAB5A: P20339
Identifier: R-HSA-8875323
Species: Homo sapiens
Compartment: early endosome membrane
Primary external reference: UniProt: RAB5A: P20339
Identifier: R-HSA-8870432
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P20339
Identifier: R-HSA-8871125
Species: Homo sapiens
Compartment: clathrin-coated endocytic vesicle membrane
Primary external reference: UniProt: P20339

Set (1 results from a total of 1)

Identifier: R-HSA-9636678
Species: Homo sapiens
Compartment: cytosol

Complex (3 results from a total of 3)

Identifier: R-HSA-9636699
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-2130191
Species: Homo sapiens
Compartment: early endosome membrane
Identifier: R-HSA-9636689
Species: Homo sapiens
Compartment: cytosol

Reaction (3 results from a total of 3)

Identifier: R-HSA-9636684
Species: Homo sapiens
Compartment: cytosol
Ras-related protein with guanosine 5'-triphosphates bound to GTP (RAB5A:GTP,RAB7A:GTP) get deactivated through dephosphorylation of GTP via the GTPase-activating protein (GAP)-like activity of the Mtb nucleoside diphosphate kinase (ndkA) (Chopra et al. 2004, Sun et al. 2010).
Identifier: R-HSA-6801109
Species: Homo sapiens
Compartment: cytosol, plasma membrane
RAB escort protein CHM (REP1) binds the RAB geranylgeranyl transferase complex, RGGT, composed of RABGGTA and RABGGTB (Baron and Seabra 2008). The interaction between CHM and the RGGT complex is enhanced by the presence of phosphoisoprenoids (Thoma et al. 2001). The complex of RGGT and CHM catalyzes geranylgeranylation of small GTPases RAB1A, RAB3A and RAB5A, which is needed for the membrane localization of RABs (Farnsworth et al. 1994). RAB geranylgeranyl transferase can play an anti-apoptotic role, through an unknown mechanism (Lackner et al. 2005). RAB5A, the substrate of RGGT:CHM complex, was shown to positively regulate formation of autophagosomes (Li et al. 2013).
Identifier: R-HSA-8870469
Species: Homo sapiens
Compartment: cytosol
RAB geranylgeranyltransferase (GGTase) recognizes and geranylgeranylates cysteine residues in -CXCX, -CCXX or -XXCC motifs in the C-termini of RAB proteins. Most RAB proteins are doubly geranylgeranylated, most likely in a sequential fashion, but some are only singly modified (Baron and Seabra, 2008; Farnsworth et al 1994; Wilson et al, 1996; Overmeyer et al, 2000; Khosravi-Far et al, 1991; Joberty et al, 1993; Catherman et al, 2013; Leung et al, 2007; Maurer-Stroh et al, 2007). In most cases, geranylgeranylation is required for proper localization and function of the RAB proteins. After geranylgeranylation, RABs remain associated with the RAB escort protein CHM or CHML, which dissociates when the GTPase reaches its target membrane (Alexandrov et al, 1994; Seabra et al, 1996; Shen and Seabra, 1996). Release of the geranylgeranyl RAB:CHM complex from the catalytic subunits is promoted by the binding of additional GGPP to the enzyme (Baron and Seabra, 2008). Once prenylated, RABs cycle between active GTP bound forms that are membrane associated, and inactive GDP bound forms that are cytosolic and associated with RAB GDP dissociation inhibitor (GDI) proteins. Conversion between these states is governed by the activities of guanine nucleotide exchange factors (GEFs), which promote the exchange of GDP for GTP, and GTPase activating proteins (GAPs), which stimulate the intrinsic GTPase activity of RABs (Ullrich et al, 1993; Soldati et al, 1994; reviewed in Wandinger-Ness and Zerial, 2014; Stenmark, 2009).

Pathway (2 results from a total of 2)

Identifier: R-HSA-8873719
Species: Homo sapiens
Human cells have more than 60 RAB proteins that are involved in trafficking of proteins in the endolysosomal system. These small GTPases contribute to trafficking specificity by localizing to the membranes of different endocytic compartments and interacting with effectors such as sorting adaptors, tethering factors, kinases, phosphatases and tubular-vesicular cargo (reviewed in Stenmark et al, 2009; Wandinger-Ness and Zerial, 2014). RAB localization depends on a number of factors including C-terminal prenylation, the sequence of an upstream hypervariable regions and what nucleotide is bound (Chavrier et al, 1991; Ullrich et al, 1993; Soldati et al, 1994; Farnsworth et al, 1994; Seabra, 1996; Wu et al, 2010; reviewed in Stenmark, 2009; Wandinger-Ness and Zerial, 2014). In the active, GTP-bound form, prenylated RAB proteins are membrane associated, while in the inactive GDP-bound form, RABs are extracted from the target membrane and exist in a soluble form in complex with GDP dissociation inhibitors (GDIs) (Ullrich et al, 1993; Soldati et al, 1994; Gavriljuk et al, 2103). Conversion between the inactive and active form relies on the activities of RAB guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs) (Yoshimura et al, 2010; Wu et al, 2011; Pan et al, 2006; Frasa et al, 2012; reviewed in Stenmark, 2009; Wandinger-Ness and Zerial, 2014).
Newly synthesized RABs are bound by a RAB escort protein, CHM (also known as REP1) or CHML (REP2) (Alexandrov et al, 1994; Shen and Seabra, 1996). CHM/REP proteins are the substrate-binding component of the trimeric RAB geranylgeranyltransferase enzyme (GGTaseII) along with the two catalytic subunits RABGGTA and RABGGTB (reviewed in Gutkowska and Swiezewska, 2012; Palsuledesai and Distefano, 2015). REP proteins recruit the unmodified RAB in its GDP-bound state to the GGTase for sequential geranylgeranylation at one or two C-terminal cysteine residues (Alexandrov et al, 1994; Seabra et al 1996; Shen and Seabra, 1996; Baron and Seabra, 2008). After geranylgeranylation, CHM/REP proteins remain in complex with the geranylgeranylated RAB and escort it to its target membrane, where its activity is regulated by GAPs, GEFs, GDIs and membrane-bound GDI displacement factors (GDFs) (Sivars et al, 2003; reviewed in Stenmark, 2009; Wandinger-Ness and Zerial, 2014).
Identifier: R-HSA-8876198
Species: Homo sapiens
Human cells have more than 60 RAB proteins that are key regulators of intracellular membrane trafficking. These small GTPases contribute to trafficking specificity by localizing to the membranes of different organelles and interacting with effectors such as sorting adaptors, tethering factors, kinases, phosphatases and tubular-vesicular cargo (reviewed in Stenmark et al, 2009; Wandinger-Ness and Zerial, 2014; Zhen and Stenmark, 2015).

RAB localization depends on a number of factors including C-terminal prenylation, the sequence of upstream hypervariable regions and what nucleotide is bound, as well as interaction with RAB-interacting proteins (Chavrier et al, 1991; Ullrich et al, 1993; Soldati et al, 1994; Farnsworth et al, 1994; Seabra, 1996; Wu et al, 2010; reviewed in Stenmark, 2009; Wandinger-Ness and Zerial, 2014). More recently, the activity of RAB GEFs has also been implicated in regulating the localization of RAB proteins (Blumer et al, 2103; Schoebel et al, 2009; Cabrera and Ungermann, 2013; reviewed in Barr, 2013; Zhen and Stenmark, 2015)

In the active, GTP-bound form, RAB proteins are membrane-associated, while in the inactive GDP-bound form, RABs are extracted from the target membrane and exist in a soluble form in complex with GDP dissociation inhibitors (GDIs) (Ullrich et al, 1993; Soldati et al, 1994; Gavriljuk et al, 2013). Conversion between the inactive and active form relies on the activities of RAB guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs) (Yoshimura et al, 2010; Wu et al, 2011; Pan et al, 2006; Frasa et al, 2012; reviewed in Stenmark, 2009; Wandinger-Ness and Zerial, 2014; Ishida et al, 2016).

Newly synthesized RABs are bound to a RAB escort protein, CHM (also known as REP1) or CHML (REP2) (Alexandrov et al, 1994; Shen and Seabra, 1996). CHM/REP proteins are the substrate-binding component of the trimeric RAB geranylgeranyltransferase enzyme (GGTaseII) along with the two catalytic subunits RABGGTA and RABGGTB (reviewed in Gutkowska and Swiezewska, 2012; Palsuledesai and Distefano, 2015). REP proteins recruit the unmodified RAB in its GDP-bound state to the GGTase for sequential geranylgeranylation at one or two C-terminal cysteine residues (Alexandrov et al, 1994; Seabra et al 1996; Shen and Seabra, 1996; Baron and Seabra, 2008). After geranylation, CHM/REP proteins remain in complex with the geranylated RAB and escort it to its target membrane, where RAB activity is regulated by GAPs, GEFs, GDIs and membrane-bound GDI displacement factors (GDFs) (Sivars et al, 2003; reviewed in Stenmark, 2009; Wandinger-Ness and Zerial, 2014).

Unlike the RAB GAPS, which (to date) all contain a shared TBC domain, RAB GEFs are structurally diverse and range from monomeric to multisubunit complexes (reviewed in Fukuda et al, 2011; Frasa et al, 2012; Cherfils and Zeghouf, 2013; Ishida et al, 2016). While many GEFs contain one of three conserved GEF domains identified to date - the DENN (differentially expressed in normal and neoplastic cell) domain, the VPS9 domain and the SEC2 domain- other GEFs lack a conserved domain (reviewed in Ishida et al, 2016). Based on sequence conservation and subunit organization, GEFs can be grouped into 6 general classes: the DENND-containing GEFs, the VPS9-containing GEFs (both monomeric), the SEC2-containing GEFs (homodimeric), heterodimeric GEF complexes such as RIC1:RGP1, the multisubunit TRAPPC GEF, and others (reviewed in Barr and Lambright, 2010; Marat et al, 2011; Ishida et al, 2016). GEFs for many RABs have still not been identified, however.
Cite Us!