XB-FEAT-481451: Difference between revisions
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Cysteine-rich motor neuron 1 (CRIM1) was originally identified as a partial cDNA in an interaction screen [11] and in a screen for secreted proteins (C. Tabin, personal communication). Assembly of the full sequence representing the CRIM1 cDNA [11] revealed that it was a type 1 trans-membrane protein with N-terminal homology to insulin-like growth factor binding domains (IGFBP; [11], [12]) and a set of six cysteine-rich von Willebrand factor C (vWC) repeats occupying the remaining extracellular domain. The cysteine-rich repeats of CRIM1 are similar to those of chordin [13] and its Drosophila homolog, short gastrulation [14] that can bind bone morphogenetic proteins (BMPs) [15], [16]. Another protein that contains an IGFBP and single cysteine-rich domain is Cyr61, a secreted heparin binding, extracellular matrix associated protein that is required for normal gastrulation movements [17]. CRIM1 is expressed in a variety of tissues and cell types that include the vertebrate CNS [11] urogenital tract [18] eye [19], [20] and vascular system [21]. CRIM1 protein has been localized to the endoplasmic reticulum [21], [22] or to junctional complexes upon stimulation of vascular endothelial cells [21]. | "Cysteine-rich motor neuron 1 (CRIM1) was originally identified as a partial cDNA in an interaction screen [11] and in a screen for secreted proteins (C. Tabin, personal communication). Assembly of the full sequence representing the CRIM1 cDNA [11] revealed that it was a type 1 trans-membrane protein with N-terminal homology to insulin-like growth factor binding domains (IGFBP; [11], [12]) and a set of six cysteine-rich von Willebrand factor C (vWC) repeats occupying the remaining extracellular domain. The cysteine-rich repeats of CRIM1 are similar to those of chordin [13] and its Drosophila homolog, short gastrulation [14] that can bind bone morphogenetic proteins (BMPs) [15], [16]. Another protein that contains an IGFBP and single cysteine-rich domain is Cyr61, a secreted heparin binding, extracellular matrix associated protein that is required for normal gastrulation movements [17]. CRIM1 is expressed in a variety of tissues and cell types that include the vertebrate CNS [11] urogenital tract [18] eye [19], [20] and vascular system [21]. CRIM1 protein has been localized to the endoplasmic reticulum [21], [22] or to junctional complexes upon stimulation of vascular endothelial cells [21]. | ||
Analysis of CRIM1 function suggested it has a role in vascular tube formation both in culture [21] and in vivo in the fish [23]. Consistent with expression of CRIM1 in the neural tube [11], over-expression of the CRIM1 ectodomain in the chick neural tube reduces the numbers of certain spinal cord neurons [20]. CRIM1 was also been proposed to be an antagonist for bone morphogenetic proteins (BMPs) through suppression of BMP maturation and sequestration in the Golgi or at the cell surface [22]. This activity is dependent upon the extracellular vWC repeats [22]. Expression of CRIM1 in the chick neural tube was, however, insufficient to modulate ventral patterning [20] where BMP activity is critical [24]. An assessment of the function of crm-1, a C. elegans homologue of CRIM1, has suggested a role in enhancing BMP signaling [25]. Identification of a CRIM1 hypomorphic mutant in the mouse (CRIM1KST264, [26]) that was generated by lacz insertional mutagenesis has revealed that CRIM1 is involved in the development of multiple organ systems including the limbs, eye and kidney vascular system [26], [27]. | Analysis of CRIM1 function suggested it has a role in vascular tube formation both in culture [21] and in vivo in the fish [23]. Consistent with expression of CRIM1 in the neural tube [11], over-expression of the CRIM1 ectodomain in the chick neural tube reduces the numbers of certain spinal cord neurons [20]. CRIM1 was also been proposed to be an antagonist for bone morphogenetic proteins (BMPs) through suppression of BMP maturation and sequestration in the Golgi or at the cell surface [22]. This activity is dependent upon the extracellular vWC repeats [22]. Expression of CRIM1 in the chick neural tube was, however, insufficient to modulate ventral patterning [20] where BMP activity is critical [24]. An assessment of the function of crm-1, a C. elegans homologue of CRIM1, has suggested a role in enhancing BMP signaling [25]. Identification of a CRIM1 hypomorphic mutant in the mouse (CRIM1KST264, [26]) that was generated by lacz insertional mutagenesis has revealed that CRIM1 is involved in the development of multiple organ systems including the limbs, eye and kidney vascular system [26], [27]." | ||
Latest revision as of 07:51, 6 December 2016
crim1
This is the community wiki page for the gene crim1 please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase
nomenclature changes
previously called Cysteine-rich motor neuron 1
functional information
from XB-art-45000 "Cysteine-rich motor neuron 1 (CRIM1) was originally identified as a partial cDNA in an interaction screen [11] and in a screen for secreted proteins (C. Tabin, personal communication). Assembly of the full sequence representing the CRIM1 cDNA [11] revealed that it was a type 1 trans-membrane protein with N-terminal homology to insulin-like growth factor binding domains (IGFBP; [11], [12]) and a set of six cysteine-rich von Willebrand factor C (vWC) repeats occupying the remaining extracellular domain. The cysteine-rich repeats of CRIM1 are similar to those of chordin [13] and its Drosophila homolog, short gastrulation [14] that can bind bone morphogenetic proteins (BMPs) [15], [16]. Another protein that contains an IGFBP and single cysteine-rich domain is Cyr61, a secreted heparin binding, extracellular matrix associated protein that is required for normal gastrulation movements [17]. CRIM1 is expressed in a variety of tissues and cell types that include the vertebrate CNS [11] urogenital tract [18] eye [19], [20] and vascular system [21]. CRIM1 protein has been localized to the endoplasmic reticulum [21], [22] or to junctional complexes upon stimulation of vascular endothelial cells [21].
Analysis of CRIM1 function suggested it has a role in vascular tube formation both in culture [21] and in vivo in the fish [23]. Consistent with expression of CRIM1 in the neural tube [11], over-expression of the CRIM1 ectodomain in the chick neural tube reduces the numbers of certain spinal cord neurons [20]. CRIM1 was also been proposed to be an antagonist for bone morphogenetic proteins (BMPs) through suppression of BMP maturation and sequestration in the Golgi or at the cell surface [22]. This activity is dependent upon the extracellular vWC repeats [22]. Expression of CRIM1 in the chick neural tube was, however, insufficient to modulate ventral patterning [20] where BMP activity is critical [24]. An assessment of the function of crm-1, a C. elegans homologue of CRIM1, has suggested a role in enhancing BMP signaling [25]. Identification of a CRIM1 hypomorphic mutant in the mouse (CRIM1KST264, [26]) that was generated by lacz insertional mutagenesis has revealed that CRIM1 is involved in the development of multiple organ systems including the limbs, eye and kidney vascular system [26], [27]."