The muniscin protein family was initially defined in 2009 [4] as proteins having 2 homologous domains that are involved in clathrin mediated endocytosis (CME) and have been reviewed. [5] In addition to FCHO1, FCHO2 and Syp1, [6] [7] SGIP1 is also included in the family because it contains the μ (mu) homology domain and is involved in CME, even though it does not contain the F-BAR domain [1] [8]
Muniscins are known as alternate cargo adaptors. That is, they participate in selecting which cargo molecules are internalized via CME. [5] Additionally, the structure of the dimer, with its concave face oriented toward the plasma membrane, is thought to help curve the membrane as the clathrin coated pit forms. [5] The muniscins are early arriving proteins involved in CME. [5] FCHO proteins are required for CME, [9] but do not appear to be required to initiate CME. [10]
The μ homology domain of muniscins has been reported to have evolved from part of an ancient cargo adaptor protein complex named TSET. [11]
The muniscin protein family was initially defined in 2009 [4] as proteins having 2 homologous domains that are involved in clathrin mediated endocytosis (CME) and have been reviewed. [5] In addition to FCHO1, FCHO2 and Syp1, [6] [7] SGIP1 is also included in the family because it contains the μ (mu) homology domain and is involved in CME, even though it does not contain the F-BAR domain [1] [8]
Muniscins are known as alternate cargo adaptors. That is, they participate in selecting which cargo molecules are internalized via CME. [5] Additionally, the structure of the dimer, with its concave face oriented toward the plasma membrane, is thought to help curve the membrane as the clathrin coated pit forms. [5] The muniscins are early arriving proteins involved in CME. [5] FCHO proteins are required for CME, [9] but do not appear to be required to initiate CME. [10]
The μ homology domain of muniscins has been reported to have evolved from part of an ancient cargo adaptor protein complex named TSET. [11]